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LAUNDRY DETERGENT ANDIOR FABRIC CARE COMPOSITIONS
COMPRISING A MODIFIED CEI_LULASE
Field of the Invention
The present invention relates to laundry detergent and/or fabric care
compositions comprising a modified enzyme which comprises a catalytically
active amino acid sequence of a cellulolytic enzyme linked to an amino acid
sequence comprising a Cellulose Binding Domain (CBD) having a relative
binding constant (Kr-aj for binding to amorphous cellulose higher than
2.41/gcellulose, preferably higher than 3.51lgcellulose, more preferably
higher
than 4 Ilgcellulose.
Background of the invention
Detergent compositions include nowadays a complex combination of active
ingredients and in particular, detergent enzymes such as cellulases.
The activity of cellulase is one in which cellulo:~ic fibres or substrates are
attacked by the cellulase and is depending on the particular function of the
cellulase, which can be endo- or exo- cellulase and on the respective
hemicellulases. The cellulose structures are dep~olymerized or cleaved into
smaller and thereby more soluble or dispersible fractions. This activity in
particular on fabrics provides cleaning, rejuvenation, softening and generally
improved handfeel characteristics to the fabric structure. This has been
previously speculated to be the result of the cleavage of fibrils from the
surface
of fibres such that the main strand of the fibre beconnes smoother, less
available
for incrustation, less likely to entangle with other fibers and optically less
diffuse
in its light reflecting and emission.
Improvements in the activity of particular cellulase compositions have been
made over time in order to allow lower usage or shorter exposure times for
similar benefits. In the detergent feld, cellulase~s performing in a typical
detergent wash environment are available with an <~ctivity at which the
desired
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cellulase performance is reached prior to the end of a wash-cycle. However,
since the cellulase continues to react, even after having provided the desired
performance, cleavage of the cellulose will continue. Therefore, there is a
potential risk of tensile strength loss. .
It should be noted however, that tensile strength loss of fabric is also an
unavoidable result of mechanical action due to u:>e/wearing and may further
result from damage by a bleaching component in they laundry process,
especially
if the fabric is contaminated with metal compounds.
The object of the present invention is to provide laundry detergent andlor
fabric
care compositions which achieve excellent fabric care, including anti-wrinkle,
anti-bobbling and anti-shrinkage properties to fabrics, as well as provide
static
control, fabric softness, colour appearance and fabric anti-wear properties
and
benefits, and which achieve excellent fabric cleaning while preventing tensile
strength loss.
The above objective has been met by formulating laundry detergent and/or
fabric care compositions comprising a modified enzyme which comprises a
catalytically active amino acid sequence of a cellulolytic enzyme linked to an
amino acid sequence comprising a Cellulose Binding Domain (CBD) haring a
relative binding constant (Kr-a) for binding to amorphous cellulose higher
than
2.41/gcellulose, preferably higher than 3.51lgcelluloae, more preferably
higher
than 4l/gcellulose.
W091110732 discloses an enzyme which exhibits c:ellulase activity, producible
by a strain of Bacillus spp., NICMB 40250, especially an 75, 56 or 45 kD
Molecular weight endoglucanase or characterised bay a high specific activity
for
e.g. detergency application, providing softening, soil removal and colour
clarification. Novel derivatives of celiulase enzyme:; combining a core region
derived from said endoglucanase with a CBD derived from another cellulase
enzyme or a combining a core region derived from another cellulase enzyme
with a CBD derived from said endoglucanase, are therein contemplated to
construct cellulase enzymes with improved binding properties.
W094/07998 describes cellulase variants of a cellullase classified in family
45,
comprising a CBD, a Catalytically Active Domain (CAD) and a region finking the
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CBD to the CAD, wherein one or more amino acid residues have been added,
deleted or substituted andlor another CBD is added at the opposite end of the
CAD. These enzymes have improved propertie:> such as alkaline activity,
harshness reduction, compatibility with detergent ingredients, particulate
soil
removal, colour clarification, defuzzing, depilling, harshness reduction and
sensitivity to anionic surfactants and peroxidase bleaching systems and are
useful in detergent compositions.
W095I16782 relates to the cloning and high level expression of novel truncated
cellulose proteins or derivatives thereof in Tn~choderma longibrachiatum.
Combinations of different core regions with severail CBDs are described in the
fibrelfabric context.
A cellulolytic enzyme preparation comprising a cellulose with reduced
mobility,
e.g. by increasing the molecular weight ar apparent size of the cellulose
protein
molecule or by insolubilising or immobilising the cellulose, has been
disclosed in
W097/01629. The mobility of the cellulose component may be reduced by
adsorption to an insoluble or soluble carrier e.g" via the existing or newly
introduced CBD.
However, none of these documents disclose a modifiied enzyme which
comprises a catalytically active amino acid sequence of a celluloiytic enzyme
linked to an amino acid sequence comprising a Cellulose Binding Domain
having a Kr-a of a definite va#ue, thereby defining a cellulose especially
adapted
to selectively bind and hydrolyse amorphous cellulose of cotton containing
fabrics for a laundry and/or fabric care application.
Summaryr of the invention
The present invention relates a modified cellulolytic enzyme demonstrating
selective binding and hydrolysis of amorphous cellulose in cotton containing
fabrics. The present invention further relates to a laundry detergent andlor
fabric
care composition comprising said modified enzyme. Said compositions achieve
excellent fabric care and fabric cleaning while preventing tensile strength
loss.
This modified enzyme comprises a catalytically active amino acid sequence of a
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cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose
Binding Domain {CBD) having a relative binding constant (Kr-a) for binding to
amorphous cellulose higher than 2.41/gcellulose, preferably higher than
3.51/gcellulose, more preferably higher than 4l/gcellulose.
In a further embodiment of the present invention, the' present invention
relates to
a modified enzyme which comprises a catalytically active amino acid sequence
of a cellulolytic enzyme linked to an amino acid sequence comprising a
Cellulose Binding Domain further characterised by having a relative binding
constant for bacterial microcrystalline cellulose (Kr-c) lower than
1l/gcellulose,
preferably lower than 0.5i/gcellulose.
More preferably, the modified enzyme of the present invention, comprises a
catalytically active amino acid sequence of a cellulolytic enzyme linked to an
amino acid sequence comprising a Cellulose Binding Domain further
characterised by having a relative binding cone~tant (Kr-a) for binding to
amorphous cellulose to a relative binding constant lfor bacterial
microcrystalline
cellulose (Kr-c) ratio above 3.
The present invention further relates to laundry detergent and/or fabric care
compositions comprising said modified enzyme and which preferably further
comprise a detergent ingredient selected from cationic surfactants, dye
transfer
inhibiting polymer, builders, - in particular zeolite A and sodium
tripolyphosphate
andlor clays .
Detailed description of the invention
The present invention relates to a modified enzyme which comprises a
catalytically active amino acid sequence of a ceiluilolytic enzyme linked to
an
amino acid sequence comprising a cellulose binding domain having a relative
binding constant for binding to amorphous cellulose higher than
2.411gcellulose,
preferably higher than 3.511gcellulose, more preferably higher than 4
Ilgcellulose.
Cellulolytic enzyme
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A modified enzyme for use in accordance with the present invention comprises a
catalytically active (enzymatically active) amino acid sequence {in general a
polypeptide amino acid sequence) of a cellulolytic enzyme linked to an amino
acid sequence comprising a Cellulose Binding Domain having a high affinity for
binding to amorphous cellulose.
The catalytically active amino acid sequence in question may comprise or
consist of the whole of - or substantially the whole of - the full amino acid
sequence of the mature enzyme in question, or it may consist of a portion of
the
full sequence which retains substantially the same catalytic (enzymatic)
properties as the full sequence.
Modified enzymes (enzyme hybrids) of the type in question, as well as detailed
descriptions of the preparation and purification thereof, are known in the art
[see, e.g., WO 90/00609, WO 94/24158 and 1N0 95116782, as well as
Greenwood et al., Biotechnology and Bioeng~inee~ri_ ngi 44, (1994) pp. 1295 -
1305j. The praduction of enzymes hybrid is described in WO 91/10732 wherein
novel derivatives of cellulase enzymes combining a core region derived from a
Bacillus NICB 40250 endoglucanase with a CBD derived from another cellulase
enzyme or a combining a core region derived from another ceilulase enzyme
with a CBD derived from a Bacillus NICB 40250 endoglucanase, are
constructed. WO 95/16782 describes the combinatiions of different core regions
with several CBD and the cloning and high level expression of these novel
truncated cellulase proteins or derivatives thereof, in Trichoderma
longibrachiatum.
They may, e.g., be prepared by transforming into .a host cell a DNA construct
comprising at least a fragment of DNA encoding the cellulose-binding domain
ligated, with or without a Pinker, to a DNA sequence encoding the enzyme of
interest, and growing the transformed host cell to express the fused gene. One
relevant, but non-limiting, type of recombinant product (enzyme hybrid)
obtainable in this matter - often referred to in the art as a "fusion
protein'" - may
be described by one of the following general formulae:
A-CBD-MFL-X-B
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A-X-MR-CBD-B
In the latter formulae, CBD is an amino acid sequence comprising at least the
cellulose-binding domain (CBD) per se.
MR (the middle region; a linking region) may be a bond, or a linking group
comprising from 1 to about 100 amino acid residue~~, in particular of from 2
to 40
amino acid residues, e.g. from 2 to 15 amino aicid residues. MR may, in
principle, alternatively be a non-amino-acid linker (See below).
X is an amino acid sequence cor~iprising the above-mentioned, catalytically
(enzymatically) active sequence of amino acid residues of a polypeptide
encoded by a DNA sequence encoding the cellulol~tic enzyme of interest.
The moieties A and B are independently optional. lNhen present, a moiety A or
B constitutes a terminal extension of a CBD or X moiety, and normally
comprises one or more amino acid residues.
It will thus, inter alia, be apparent from the above: that a CBD in an enzyme
hybrid of the type in question may be positioned C-terminally, N-terminally or
internally in the enzyme hybrid. Correspondingly, an X moiety in an enzyme
hybrid of the type in question may be positioned N-terminally, C-terminally,
or
internally in the enzyme hybrid.
Enzyme hybrids of interest in the context of thE; invention include enzyme
hybrids which comprise more than one CBD, e.g. :such that two or more CBDs
are linked directly to each other, or are separated from one another by means
of
spacer or linker sequences (consisting typically of a sequence of amino acid
residues of appropriate length. Two CBDs in an enzyme hybrid of the type in
question may, for example, also be separated from one another by means of an
-MR-X- moiety as defined above. One or more cellulose binding domain can be
linked to the N-terminal andlor C-terminal parts of the cellulase core region.
Any
part of a CBD can be selected, modified, truncated E~tc.
Preferably, attention will be given in the construction of enzyme hybrids of
the
type in question to the stability towards proteolytic degradation. Two- and
multi-
domain proteins are particularly susceptible towards proteolytic cleavage of
linker regions connecting the domains. Proteases causing such cleavage may,
for example, be subtilisins, which are known to often exhibit broad substrate
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specificities [see, e.g. : Grr~n et al., Biochemistry 31 (1992), pp. 6011-
6018;
Teplyakov et al., Protein Enaineerinc 5 (1992), pp. 413-420]. Glycosylation of
linker residues in eukaryotes is one Nature's ways of preventing proteolytic
degradation. Another is to employ amino acids which are less favoured by the
surrounding proteases. The length of the linker also plays a role in relation
to
accessibility by proteases. Which "solution" is optimal depends on the
environment in which the enzyme hybrid is to function. When constructing new
enzyme hybrid molecules, preferably attention will be paid to the linker
stability.
Plasmids
Preparation of plasmids capable of expressing fusion proteins having the amino
acid sequences derived from fragments of more than one poiypeptide is well
known in the art (see, for example, WO 90J0060~9 and WO 95/16782). The
expression cassette may be included within a replication system for episomal
maintenance in an appropriate cellular host or may be provided without a
replication system, where it rnay become integratecl into the host genome. The
DNA may be introduced into the host in accordance with known techniques such
as transformation, microinjection or the like.
Once the fused gene has been introduced into the appropriate host, the host
may be grown to express the fused gene. Normally it is desirable additionally
to
add a signal sequence which provides for secretion of the fused gene. Typical
examples of useful genes are
1) Signal sequence -- (pro-peptide) -- carbohydratE;-binding domain -- linker -
-
enzyme sequence of interest, or
2) Signal sequence -- (pr~-peptide} -- enzyme sequence of interest -- linker --
carbohydrate-binding domain,
in which the pro-peptide sequence normally contains 5-100, e.g. 5-25, amino
acid residues. The recombinant product may be glycosylated or non-
glycosylated.
Celiulolytic enzymes
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Any enzyme which exhibits a cellulase activity is suitable for the purpose of
the
present invention and includes cellulases without naturally occurring CBD,
cellulase to which a CBD of Kr-a for binding to amorphous cellulose higher
than
2.411gcellulose, preferably higher than 3.511gcellulose, more preferably
higher
than 4 IIgceHulose, is added and/or cellulases having a CBD presenting a lower
Kr value, to which a CBD of Kr-a higher than 2.411gcellulose, preferably
higher
than 3.51/gcellulose, more preferably higher than 4 Ilgcellulose, is then
substituted or added.
The catalytically active amino acid sequence of a cellulolytic enzyme can be
derived from any cellulase. The cellulases usablEe in the present invention
include both bacterial or fungal cellulases. Preferably, they will have a pH
optimum of between 5 and 12 and a specific activity above 50 CE9/Ulmg
(Cellulose ~Aiscosity Unit). Suitable cellulases arE: disclosed in U.S. Patent
4,435,307, Barbesgoard et al, J61078384 and W096102653 which discloses
fungal cellulase produced respectively from Huminola insolens, Trichoderma,
Thielavia and Sporotrichum. EP 739 982 describes cellulases isolated from
novel Bacillus species. Suitable cellulases are also disclosed in GB-A-
2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and W095I26398.
Examples of such cellulases are cellulases produced by a strain of Humicola
insolens (Humicola grisea var. thermoidea), particulairly the Numicola strain
DSM
1800. Other suitable cellulases are cellulases originated from Humicola
insolens
having a molecular weight of about 50KDa, an isoelectric point of 5.5 and
containing 415 amino acids; and a -43kD endoglucanase derived from Humicola
insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase
component has the amino acid sequence disclosed in PCT Patent Application
No. WO 91/17243. Also suitable cellulases are the EG111 cellulases from
Trichoderma longibrachiatum described in W094/21801, Genencor, published
September 29, 1994. Especially suitable cellulases are the cellulases having
colour care benefits. Examples of such cellulases are cellulases described in
European patent application No. 91202879.2, filed November 6, 1991 (Novo).
Carezyme and Celluzyme (Novo Nordisk A/S) are especially useful. See also
W091117244 and W091/21801. Other suitable cellulases for fabric care andlor
cleaning properties are described in W096/34092, W096I17994 and
W095/24471.
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Preferred catalytically active amino acid sequences of a celluiolytic enzyme
for
the laundry detergent andlor fabric care compositions of the present invention
are producible by a fungal strain, preferably produced by a strain of Humicola
insolens and more preferably is a "43kD endoglucanase derived from Hr~micola
insolens, DSM 1800, exhibiting cellulose activity.
Said modified cellulolytic enzymes are normally incorporated in the laundry
detergent and/or fabric care composition at levels from 0.0001 % to 2%,
preferably 0.0001 % to 0.5%, more preferably 0.000.5% to 0.1 % of pure
modified
enzyme by vveight of the detergent composition.
Preferred catalytically active amino acid sequence of a cellulolytic enzyme
for
specific applications are derived from alkaline celluiases, i.e. enzymes
having an
enzymatic activity of at least 10%, preferably at least 25%, more preferably
at
least 40% of their maximum activity at a pH ranging from 7 to 12, preferably
10.5. More preferred core cellulases are enzymes having their maximum activity
at a pH ranging from 7 to 12, preferably 10.5.
The above-mentioned enzymes may be of any suitable origin, such as
vegetable, animal, bacterial, fungal and yeast origin. Origin can further be
mesophilic or extremophilic (psychrophilic, ps,ychrotrophic, thermophilic,
barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-
purified forms
of these enzymes may be used. Nowadays, it is common practice to modify wild-
type enzymes via protein / genetic engineering techniques in order to optimise
their performance efficiency in the laundry dei;ergent andlor fabric care
compositions of the invention. For example, the variants may be designed such
that the compatibility of the enzyme to commonly encountered ingredients of
such compositions is increased. Alternatively, the variant may be designed
such
that the optimal pH, bleach or chelant stability, catalytic activity and the
like, of
the enzyme variant is tailored to suit the particular clE~aning application.
In particular, attention should be focused on amino acids sensitive to
oxidation in
the case of bleach stability and on surface charges for the surfactant
compatibility. The isoelectric point of such enzyme's may be modified by the
substitution of some charged amino acids, e.g. an increase in isoelectric
point
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may help to improve compatibility with anionic surfactants. The stability of
the
enzymes may be further enhanced by the creation of e.g. additional salt
bridges
and enforcing metal binding sites to increase cheian~t stability.
Cellulose Binding Domain (CBD}
Cellulose Binding Domains
fn the present context, the terms "amino acid sequence comprising a CBD,
Cellulose Binding Domain or CBD" are intended to indicate an amino acid
sequence capable of effecting binding of the cellul;ase to a cellulosic
substrate
(e.g., as described in P. Kraulis et al., Determination of the three-
dimensional
structure of the C terminal domain of cellobiohydrolase I from Trichoderma
reesei. A study using nuclear magnetic resonance and hybrid distance
geometry-dynamically simulated annealing. Biochemistry 28:7241-7257, 1989).
The classification and properties of cellulose binding domains are presented
in
P. Tomme et al., in the symposium "Enzymatic degradation of insoluble
polysaccharides" (ACS Symposium Series 618, edited by ,i.N. Saddler and M.H.
Penner, ACS, 1995).
Cellulose-binding (and other carbohydrate-binding} domains are polypeptide
amino acid sequences which occur as integral parts of large polypeptides or
proteins consisting of two or more polypeptide amino acid sequence regions,
especially in hydrolytic enzymes (hydrolases) which ilypically comprise a
catalytic
domain containing the active site for substrate hydrolysis and a carbohydrate-
binding domain for binding to the carbohydrate substrate in question. Such
enzymes can comprise more than one catalytic domain and one, two or three
carbohydrate-binding domains, and they may further comprise one or more
polypeptide amino acid sequence regions linkinc; the carbohydrate-binding
domains) with the catalytic domain(s), a region of i;he latter type usually
being
denoted a "linker".
Examples of hydrolytic enzymes comprising a cellulose-binding domain are
cellulase, xylanases, mannanases, arabinofuranosidases, acetylesterases and
chitinases. "Cellulose-binding domains" have also been found in algae, e.g. in
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the red alga porphyra purpurea in the form of a non-hydrolytic polysaccharide-
binding protein jsee P. Tomme et al., Cellulose-binding domains -
Classification
and Properties in En~matic Degradation of Insoluble CarbohKdrates , John N.
Saddler and Michael H. Penner (Eds.}, ACS Symposium Series, No: 618
(1996)]. However, most of the known CBDs (which are classified and referred to
by P. Tomme et al. (op. cit.) as "cellulose-binding domains" derive from
cellulases and xylanases.
In the present context, the term "cellulose-binding domain" is intended to be
understood in the same manner as in the latter reference (P. Tomme et al., op.
cit. } The P. Tomme et al. reference classifies more than 120 "cellulose-
binding
domains" into 10 families (I-X) which may have dlifferent functions or roles
in
connection with the mechanism of substrate binding. However, it is to be
anticipated that new family representatives and additional families will
appear in
the future.
in proteinslpolypeptides in which CBDs occur (e.g. enzymes, typically
hydrolytic
enzymes such as cellulases), a CBD may be located at the N or C terminus or at
an internal position.
The part of a polypeptide or protein (e.g. hydrolytic enzyme) which
constitutes a
CBD per se typically consists of more than about 30 and less than about 250
amino acid residues. For example, those CBDs listed and classified in Family I
in accordance with P. Tomme et al. (op. cit.) consist of 33-37 amino acid
residues, those listed and classified in Family Ila consist of 95-108 amino
acid
residues, those listed and classified in Family VI consist of 85-92 amino acid
residues, whilst one CBD (derived from a cellulase from Clostridium
thermocellum) fisted and classified in Family VII consists of 240 amino acid
residues. Accordingly, the molecular weight of an amino acid sequence
constituting a CBD per se will typically be in the range of from about 4kD to
about 40kD, and usually below about 35kD.
Cellulose binding domains can be produced by recombinant techniques as
described in H. Stalbrand et al., Applied and Environmental Microbiology, Mar.
1995, pp. 1090-1097; E. Brun et al., (1995) Eur. J. Biochem. 237, pp. 142-148;
J.B. Coutinho et al., (1992) Molecular Microbiology 6(9,, pp. 1243-1252
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In order to isolate a cellulose binding domain of, e.g. a cellulose, several
genetic
engineering approaches may be used. One method uses restriction enzyme to
remove a portion of the gene and then to fuse the remaining gene-vector
fragment in frame to obtain a mutated gene that encodes a protein truncated
for
a particular gene fragment. Another method involves the use of exonucleases
such as Ba131 to systematically delete nucleotides either externally from the
5'
and the 3' ends of the DNA or internally from a restricted gap within the
gene.
These gene-deletion methods result in a mutated gene encoding a shortened
gene molecule whose expression product may then be evaluated for substrate-
binding (e.g. cellulose-binding) ability. Appropriate substrates for
evaluating the
binding ability include cellulosic materials such as Avicel T"" and cotton
fibres.
Other methods include the use of a selective or :specific protease capable of
cleaving a CBD, e.g. a terminal CBD, from the remainder of the polypeptide
chain of the protein in question.
As already indicated {vide supra), once a nucleotide sequence encoding the
substrate-binding (carbohydrate-binding) region has been identified, either as
cDNA or chromosomal DNA, it may then be manipulated in a variety of ways to
fuse it to a DNA sequence encoding the enzyme o~r enzymatically active amino
acid sequence of interest. The DNA fragment encoding the carbohydrate-
binding amino acid sequence, and the DNA encoding the enzyme or
enzymatically active amino acid sequence of interest are then ligated with or
without a linker. The resulting ligated DNA may then be manipulated in a
variety
of ways to achieve expression. Preferred microbial expression hosts include
certain Aspergillus species (e.g. A. niger or A. oryzae), Bacillus species,
and
organisms such as Escherichia coli or Saccharomyc:es cerevisiae.
The Cellulose Binding Domains of the present invention
The relative binding constant Kr for binding to regenerated cellulosic
(amorphous - PASC phosphoric acid swollen cellulose) or crystalline cellulose
(bacterial microcrystalline cellulose - BMCC) celiuloses at 4°C and pH
7.0 is
defined as Kr = [NO]Ka and determined from the slope of a plot of 1/[Xb] vs
11[Xf], using a double-weighted, least-squares analysis; wherein [Nd] is the
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concentration of binding sites in the absence of ligand (mol(g of cellulose)-1
), Ka
is the equi9ibrium association constant {L mol-1}, [Xb] is the concentration
of
bound ligand (mol (g of cellulose)-1 ) and [Xf] is the concentration of free
ligand
(molar) (N.R. Gilkes et al., (1992) J. Biol. Chem. ;267, pp. 6743-6749) such
as
described in P.E. Johnson et ai., (1996) Biochem. ~i5, 13895-13906.
Microcrystalline cellulose (Avicel PH101) can be obtained from FMC
International (Little Island, County. Cork, Ireland). Bacterial
rnicrocrystailine
cellulose (BMCC) can be prepared from cultures of Acetobacter xylinum (ATCC
23769) as described in Gilkes at al. 1992. Regenerated cellulose (PASO) can be
obtained by phosphoric-acid treatment of Avicel PH101 as reported in J. B.
Coutinho at al., (1992) Mol. Microbioi. 6, 1243-1252;.
Suitable CBDs for the purpose of the present invention are the CBDs derived
from a fungal or bacterial strain, preferably a bacterial strain, more
preferably
from Family Il or IV according the current classificai:ion [See P. Tomme et
al. (op
cit.)]; having a relative binding consfant (Kr-a} for binding to amorphous
cellulose
higher than 2.41lgcellulose, preferably higher than 3.51/gcellulose, more
preferably higher than 411gcellulose ceilulase.
More preferred CBDs are CBDs from family IV as. currently classified, derived
from organisms selected from Cellulomonas fi,mi, Clostridium stecorarium
(NCIMB11754), Clostridium cellulolyticum, Myxocccus xanthus, Streptomyces
reticuli andlor Thermomonospora fusca. Most preferred CBDs are the CBDs
selected from CBDs of the tandem N-terminal cellulose binding domains from
Cellulomonas ~mi [3-1,4-glucanase CenC which binds amorphous but not
crystalline cellulose (P.E. Johnson et al., (1996) Biochem. 35, 13895-13906
and
14381-14394; J.B. Coutinho et al., (1992) Molecular Microbiology 6(9), pp.
1243-1252}, CBD-dimer from Clostridium stecomrium (NCIMB11754) XynA
andlor the CBD E3 from Thermonospora fusca.
Preferably, the cellulose binding domains for tl7e purpose of the present
invention will be further characterised by having a relative binding constant
for
crystalline cellulose (Kr-c) lower than 1l/gceliul~ose, preferably lower than
0.51lgceliulose.
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More preferably, the modified enzyme of the present invention comprises a
catalytically active amino acid sequence of a cellulolytic enzyme linked to an
amino acid sequence comprising a Cellulose Binding Domain {CBD) .further
characterised by having a relative binding constant {Kr-a) for binding to
amorphous cellulose to a relative binding constant for crystalline cellulose
(Kr-c)
ratio above 3.
Even more preferably for the purpose of the present invention, the modified
enzyme comprising a catalytically active (enzymatically active) amino acid
sequence of a cellulolytic enzyme linked to CBD as defined in the present
invention, will provide an enzymatic hydrolysis activity on phosphoric acid-
swollen cellulose higher than 60 moles glucose equivalents released per minute
and per mole enzyme. Activities were determined air 37°C and pH7 (N.
Din et al.,
(1995) Prog. Biotech. 90, pp. 261-270).
Linking region
The term "linker" or "linking region" or "Middle region- MR" is intended to
indicate
a region that might adjoin the CBD and connect it to the catalytically active
amino acid sequence of the cellulolytic enzyme. When present, this linking can
be achieved chemically or by recombinant technique's.
An example of the recombinant technique describing the expression of an
enzyme with the CBD of different origin is described in S. Karita et al.,
(1996)
Journal of Fermentation and Bioengineering, Vol. 81, No. 6, pp. 553-556.
Preferred linking regions are amino acid (peptides), some examples thereof are
described in N.R. Gilkes et al., Microbiol. Rev. 55, 1991, pp. 303-315. The
linking regian can comprise from 1 to about 1 ()0 amino acid residues, in
particular of from 2 to 40 amino acid residues, e.g. from 2 to 15 amino acid
residues. As stated above, it is preferred to use amino acids which are less
favored by the surrounding proteases. Suitable amino acid linking regions are
the HumicoBa insolens family 45 cellulase linker, the NifA gene of Klebsie!!a
pneumoniae-CiP linker, the E. coli OmpA gene-CiP linker, the E3 cellulase
Thermomon~spora fusca linker and the CenA cellulase linker.; preferably the
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Humicola insoJens family 45 cellulase linker and the E3 cellulase
Thermomonospora fusca linker.
Non amino acid/proteinic compounds, referred to as "non-amino acid" can also
be used for the linking of the catalytically active .amino acid sequence to
the
CBD:
1 ) Suitable non-amino acid linking regions acre the polyethylene glycol
derivatives described in the Shearwater polymers, Inc. catalog of January
1996,
such as the nucleophilic PEGs, the carboxyl PEGs, the electrophilicaily
activated
PEGs, the sulfhydryl-selective PEGs, the heterofunctional PEGs, the biotin
PEGS, the vinyl derivatives, the PEG silanes and the PEG phospholipids. In
particular, suitable non-amino acid linking regions are the heterofunctional
PEG,
(X-PEG-Y) polymers from Shearwater such as P~EG(NPC)2, PEG-(NH2)2, t-
BOC-NH-PEG-NH2, t-BOC-NH-PEG-C02NHS, OH-PEG-NH-tBOC, FMOC-NH-
PEG-C02NHS or PEG(NPG)2 MW 3400 from Sigma, glutaric dialdehyde 50
wt% solution in water from Aldrich, disuccinimidyl suberate (DSS) form Sigma,
y-
maleimidobutyric acid N-hydroxysuccinimide ester (GMBS) from Sigma, 1-ethyl-
3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC) from Sigma and
dimethyl suberimidate hydrochloride (DMS) from Sigma.
2) Other suitable non-amino acid linking regions are 1-ethyl-3-(3-
dimethylaminopropyl) carbodiimide, N-ethyl-5-phenylisoaxolium-3-sulphonate, 1-
cyclohexyl-3(2morpholinoethyl) carbodide metho-p-toluene sulphonate, N-
ethoxycarbonyl-2-ethoxy 1,2, dihydroquinoline or glutaraldehyde.
3) Also suitable are the crosslinkers described in the 199912000 Pierce
Products
Catalogue from the Pierce Company, under the heading "Cross linking reagents
the SMPH, SMCC, LC-SMCC compounds, and preferably the Sulfo-KMUS
compound.
Preferred chemical linking regions are PEG(NPC)2, (NH2)2-PEG, t-BOC-NH-
PEG-NH2, MAL-PEG-NHS, VS-PEG-NHS polymers from Shearwater andlor the
Sulfo-KMUS compound from Pierce.
Detergent comJ~onents
The laundry detergent andlor fabric care compositions of the invention will
comprise at least one additional detergent andlor fabric care components. The
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1&
precise nature of these additional components, and levels of incorporation
thereof will depend on the physical form of the composition, and the nature of
the cleaning operation for which it is to be used.
The laundry detergent andlor fabric care compositions of the present invention
preferably further comprise a detergent ingredient selected from cationic
surfactants, dye transfer inhibiting polymers, builders - in particular
zeolite A and
sodium tripolyphosphate - and/or clays. These laundry detergent and/or fabric
care compositions achieve improved~fabric care, in<;luding improved anti-
wrinkle,
anti-bobbling and anti-shrinkage properties to fabrics, as well as provide
enhanced static control, fabric softness, colour appearance and fabric anti-
wear
properties and benefits and improved fabric cleaning while preventing tensile
strength Toss.
The laundry detergent and/or fabric care compositions according to the
invention
can be liquid, paste, gets, bars, tablets, spray, foam, powder or granular
forms.
Granular compositions can also be in "compact" norm, the liquid compositions
can also be in a "concentrated" form.
The compositions of the invention may for example, be formulated as hand and
machine laundry detergent compositions including laundry additive compositions
and compositions suitable for use in the soaking and/or pretreatment of
stained
fabrics, rinse added fabric softener compositions. Pre-or post treatment of
fabric
include gel, spray and liquid fabric care compositions. A rinse cycle with or
without the presence of softening agents is also contemplated.
iNhen formulated as compositions suitable for use in a laundry machine washing
method, the compositions of the invention preferably contain both a surfactant
and a builder compound and additionally one or more detergent components
preferably selected from organic polymeric compounds, bleaching agents,
additional enzymes, suds suppressors, dispersant:>, lime-soap dispersants,
soil
suspension and anti-redeposition agents and corrosion inhibitors. Laundry
compositions can also contain softening agenia, as additional detergent
components.
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17
The compositions of the invention can also be used as detergent additive
products in solid or liquid form. Such additivE~ products are intended to
supplement or boost the performance of conventional detergent compositions
and can be added at any stage of the cleaning process.
If needed the density of the laundry detergent compositions herein ranges from
400 to 1200 gllitre, preferably 600 to 950 g/litre of composition measured at
20°C.
The "compact" form of the compositions herein is best reflected by density
and,
in terms of composition, by the amount of inorganic filler salt; inorganic
filler salts
are conventional ingredients of detergent compositions in powder form; in
conventional detergent compositions, the filler salts are present in
substantial
amounts, typically 17-35% by weight of the total composition. In the compact
compositions, the filler salt is present in amounts not exceeding 15% of the
total
composition, preferably not exceeding 10%, most preferably not exceeding 5%
by weight of the composition. The inorganic filler salts, such as meant in the
present compositions are selected from the alkali and alkaline-earth-metal
salts
of sulphates and chlorides. A preferred filler salt is sodium sulphate.
Liquid detergent compositions according to the preaent invention can also be
in
a "concentrated form", in such case, the liquid detergent compositions
according
the present invention will contain a lower amount of water, compared to
conventional liquid detergents. Typically the water content of the
concentrated
liquid detergent is preferably less than 40%, mores preferably less than 30%,
most preferably less than 20% by weight of the detergent composition.
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Surfactant system
The laundry detergent and/or fabric care compositions according to the present
invention comprise a surfactant system wherein the surfactant can be selected
from nonionic and/or anionic and/or cationic and/or ampholytic and/or
zwitterionic and/or semi-polar surfactants. Preferred surfactants are cationic
surfactants. It has been surprisingly found that the laundry detergent and/or
fabric care compositions further comprising a .cationic surfactant, achieve
improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-
shrinkage properties to fabrics, as well as provide enhanced static control,
fabric
softness, colour appearance and fabric anti-wear properties and benefits and
improved fabric cleaning while preventing tensile strength loss.
The surfactant is typically present at a level of from 0.1 % to 60% by weight.
More preferred levels of incorporation are 1 % to 35'% by weight, most
preferably
from 1 % to 30% by weight of laundry detergent and/or fabric care compositions
in accord with the invention.
The surfactant is preferably formulated to be~ compatible with enzyme
components present in the composition. In liquid or gel compositions the
surfactant is most preferably formulated such that lit promotes, or at least
does
not degrade, the stability of any enzyme in these compositions.
Cationic detersive surfactants suitable for use in the laundry detergent
and/or
fabric care compositions of the present invention are those having one long-
chain hydrocarbyl group. Examples of such cationic surfactants include the
ammonium surfactants such as alkyltrimethylammonium halogenides, and those
surfactants having the formula
[RZ(OR3)yl~R4(OR3)yl2Rbf~+~-
wherein R2 is an alkyl or alkyl benzyl group having from about 8 to about 18
carbon atoms in the alkyl chain, each R3 is selected from the group consisting
of
-CHZCH2-, -CH2CH(CHg)-, -CH2CH(CH20H)-, -CH2CH2CH2-, and mixtures
thereof; each R4 is selected from the group consisting of C1-C4 alkyl, C1-C4
hydroxyaikyl, benzyl ring structures formed by joining the two R4 groups, -
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CH2CHOH-CHOHCOR6CHOHCH20H wherein Rf~ is any hexose or hexose
polymer having a molecular weight less than about 1000, and hydrogen when y
is not 0; R5 is the same as R4 or is an alkyl chain wherein the total number
of
carbon atoms of R~ plus R5 is not more than about 18; each y is from 0 to
about
and the sum of the y values is from 0 to about 15; and X is any compatible
anion:
Quaternary ammonium surfactant suitable for they present invention has the
formula (I):
RZ ~ s' ' ''R4
R
~~O ~Rs
,K-
Formula I
whereby R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the
formula (II)
C6-C.~ N
~CH~
O
Formula II
y is 2-4, preferably 3.
whereby R2 is H or a C1-C3 alkyl;
whereby x is 0-4, preferably 0-2, most preferably 0,
whereby R3, R4 and R5 are either the same or diifferent and can be either a
short chain alkyl (C1-C3) or alkoxylated alkyl of the formula III,
whereby X- is a counterion, preferably a halide, e.g. chloride or
methyfsulfate.
Rs
~H
O z
Formula III
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R6 is C1-C4 and z is 1 or 2.
Preferred quat ammonium surfactants are those as defined in formula t whereby
R1 is Cg, C1p or mixtures thereof, x=o,
R3, R4 = CH3 and R5 = CH2CH20H.
Highly preferred cationic surfactants are the water-soluble quaternary
ammonium compounds useful in the present composition having the formula
R1 R2R3R4N+X- (i)
wherein R1 is Cg-C1g alkyl, each of R2, R3 and R4 is independently C1-C4
alkyl, C1-C4 hydroxy alkyl, benzyl, and -(C2H40)xEi where x has a value from 2
to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl.
The preferred alkyl chain length for R1 is G12-C1;5 particularly where the
alkyl
group is a mixture of chain lengths derived from coconut or palm kernel fat or
is
derived synthetically by olefin build up or OXO alcohols synthesis. Preferred
groups for R2R3 and R4 are methyl and hydroxyeahyl groups and the anion X
may be selected from halide, methosulphate, acetaite and phosphate ions.
Examples of suitable quaternary ammonium compounds of formutae (i) for use
herein are
coconut trimethyl ammonium chloride or bromide;
coconut methyl dihydroxyethyl ammonium chloride or bromide;
decyl triethyl ammonium chloride;
decyl dimethyt hydroxyethyl ammonium chloride or bromide;
C12-15 dimethyl hydroxyethyl ammonium chloride or bromide;
coconut dimethyl hydroxyethyl ammonium chloricle or bromide;
myristyl trimethyl ammonium methyl sulphate;
lauryl dimethyl benzyl ammonium chloride or bromide;
lauryl dimethyl {ethenoxy)4 ammonium chloride c~r bromide;
choline esters (compounds of formula (i) wherein R1 is
CH2-CHI-O-C-C12-14 alkyl and R2R3R4 are methyl).
O
di-alkyl imidazolines [compounds of formula (i)].
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21
Other cationic surfactants useful herein are also described in U.S. Patent
4,228,044, Cambre, issued October 14, 1980 and in European Patent
Application EP 000,224.
Typical cationic fabric softening components include the water-insoluble
quaternary-ammonium fabric softening actives or the corresponding amine
precursor, the most commonly used having been cli-long alkyl chain ammonium
chloride or methyl sulfate.
Preferred cationic softeners among these include the following:
1} ditallow dimethylammonium chloride (DTDMAC);
2) dihydrogenated tallow dimethylammonium chloride;
3) dihydrogenated tallow dimethylammonium methylsulfate;
4) distearyl dimethylammonium chloride;
5) dioleyl dimethylammonium chloride; ,
6) dipalmityl hydroxyethyl methylammonium chloride;
7) stearyl benzyl dimethylarnmonium chloride;
8) tallow trimethylammonium chloride;
9) hydrogenated tallow trimethylammonium chloride;
10) C12-14 alkyl hydroxyethyl dimethylammonium chloride;
11 ) C12_~ g alkyl dihydroxyethyl methylammonium chloride;
12) di(stearoyioxyethyl) dimethylammonium chloride (DSOEDMAC);
13) di(tallow-oxy-ethyl) dimethylammoniunn chloride;
14) ditailow imidazolinium methylsulfate;
15} 1-(2-tallowylamidoethyl)-2-talfowyl imiciazolinium methylsulfate.
Biodegradable quaternary ammonium compounds have been presented as
alternatives to the traditionally used di-long alkyl chain ammonium chlorides
and
methyi sulfates. Such quaternary ammonium compounds contain long chain
alk(en}yl groups interrupted by functional groups such as carboxy groups. Said
materials and fabric softening compositions containing them are disclosed in
numerous publications such as EP-A-0,040,562, and EP-A-0,239,910.
The quaternary ammonium compounds and amine precursors herein have the
formula (I} or (I1), below
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22
R3 R3
R3~ /RZ _ +\i/ (CH2)rnCH -CHI X
N (C~)ri Qw'1' 1 X R3 Q
Rt T: T2
or
wherein Q is selected from -O-C(O)-, -C(O)-O-, -O-C(O)-O-, -NR4-C(O)-, -C(O)-
N R4-;
R1 is (CH2)n-Q-T2 or T3;
R2 is (CH2)m-Q-T4 or T5 or R3;
R3 is C1-C~ alkyl or C1-C~ hydroxyalkyi or H;
R4 is H or C1-C4 alkyl or C1-Cq. hydroxyalkyl;
T1, T2, T3, T4, T5 are independently C11-C22 alkyl or alkenyl;
n and m are integers from 1 to 4; and
X- is a softener-compatible anion.
Non-limiting examples of softener-compatible anions include chloride or methyl
sulfate.
The alkyl, or alkenyl, chain T1, T2, T3, T4, T~ muat contain at least 11
carbon
atoms, preferably at least 16 carbon atoms. The chain may be straight or
branched.
Tallow is a convenient and inexpensive source of long chain alkyl and alkenyl
material. The compounds wherein T1, T2, T~, T4, Tb represents the mixture of
long chain materials typical for tallow are particularly preferred.
Specific examples of quaternary ammonium compounds suitable for use in the
aqueous fabric softening compositions herein include
1) N,N-di{tallowyl-oxy-ethyl)-N,N-dimethyl ammonium chloride;
2) N,N-di{tallowyl-oxy-ethyl)-N-methyl, N-{2-hydroxyethyl) ammonium methyl
sulfate;
3) N,N-di(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl ammonium chloride;
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23
4) N,N-di(2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl)-N,N-dimethyl amrrionium
chloride; .
5) N-(2-tallowyl-oxy-2-ethyl)-N-(2-tallowyl-oxy-2-ox;o-ethyl)-N,N-dimethyl
ammonium
chloride;
6) N,N,N-tri(tallowyl-oxy-ethyl)-N-methyl ammonium chloride;
7) N-(2-tallowyi-oxy-2-oxo-ethyl)-N-(tallowyl-N,N-diimethyl-ammonium chloride;
and
8) 1,2-ditallowyl-oxy-3-trimethylamrrioniopropane chloride;
and mixtures of any of the above materials.
When included therein, the laundry detergent and/or fabric care compositions
of
the present invention typically comprise from 0.2"/° to about 25%,
preferably
from about 1 % to about 8°/~ by weight of such cationic surtactants.
Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl
phenols are suitable for use as the nonionic surfactant of the surfactant
systems
of the present invention, with the polyethylene oxide condensates being
preferred. These compounds include the condensation products of alkyl phenols
having an alkyl group containing from about 6 to about 14 carbon atoms,
preferably from about 8 to about 14 carbon atoms" in either a straight-chain
or
branched-chain configuration with the alkylene oxide. In a preferred
embodiment, the ethylene oxide is present in an amount equal to from about 2
to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene
oxide per mole of alkyl phenol. Commercially available nonionic surfactants of
this type include IgepaIT~ CO-630, marketed by the GAF Corporation; and
TritonTM X-45, X-114, X-100 and X-102, all marH;eted by the Rohm & Haas
Company. These surfactants are commonly referred to as alkylphenol
alkoxylates (e.g., alkyl phenol ethoxylates).
The condensation products of primary and secondary aliphatic alcohols with
from about 1 to about 25 moles of ethylene oxide are suitable for use as the
nonionic surfactant of the nonionic surfactant systems of the present
invention.
The alkyl chain of the aliphatic alcohol can either be straight or branched,
primary or secondary, and generally contains from about 8 to about 22 carbon
atoms. Preferred are the condensation products ~of alcohols having an alkyl
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24
group containing from about 8 to about 20 carbon atoms, more preferably from
about 10 to about 18 carbon atoms, with from ak>out 2 to about 10 moles of
ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide
and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol
'are
present in said condensation products. Examples of commercially available
nonionic surfactants of this type include TergitoIT~M 15-S-9 (the condensation
product of C11-C15 linear alcohol with 9 moles ethylene oxide), TergitoITM 24-
L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles
ethylene oxide with a narrow molecular weight distribution), both marketed by
Union Carbide Corporation; NeodoITM 45-9 (the condensation product of C14-
C15 linear alcohol with 9 moles of ethylene oxide), NeodoITM 23-3 (the
condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene
oxide), NeodoITM 45-7 {the condensation product of C14-C15 linear alcohol with
7 moles of ethylene oxide), NeodoITM 45-5 (the condensation product of C14-
C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical
Company, KyroTM EOB {the condensation product of C13-C15 alcohol with 9
moles ethylene oxide), marketed by The Procter' & Gamble Company, and
Genapol LA 030 or 050 (the condensation product of C12-C14 alcohol with 3
or 5 moles of ethylene oxide) marketed by Hoechst;. Preferred range of HLB in
these products is from 8-11 and most preferred from 8-10.
Also useful as the nonionic surfactant of the surfactant systems of the
present
invention are the alkylpolysaccharides disclosed in U.S. Patent 4,555,647,
Llenado, issued January 21, 1985, having a hydro~>hobic group containing from
about 5 to about 30 carbon atoms, preferably from abaut 10 to about 1fi carbon
atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing
from about 1.3 to about 10, preferably from about 1.3 to about 3, most
preferably
from about 1.3 to about 2.7 saccharide units., Any reducing saccharide
containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and
galactosyl moieties can be substituted for the glucosyl moieties (optionally
the
hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a
glucose or galactose as opposed to a glucoside or galactoside). The
intersaccharide bonds can be, e.g., between the one position of the additional
saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding
saccharide units.
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The preferred alkylpolyglycasides have the formula
R2o(CnH2no)t(9lYcosyl;~x
wherein R2 is selected from the group consisting of alkyl, alkylphenyl,
hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl
groups
contain from about 10 to about 18, preferably from about 12 to about 14,
carbon
atoms; n is 2 or 3, preferably 2; t is from 0 to about '10, preferably 0; and
x is
from about 1.3 to about 10, preferably from about 1.3 to about 3, most
preferably
from about 1.3 to about 2.7. The glycosyl is preferalbly derived from glucose.
To
prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed
first
and then reacted with glucose, or a source of glucose, to form the glucoside
(attachment at the 1-position). The additional glycosyl units can then be
attached between their 1-position and the precediing glycosyl units 2-, 3-, 4-
andlor 6-position, preferably predominately the 2-poaition.
The condensation products of etihylene oxide with a hydrophobic base formed
by the condensation of propylene oxide with propylene glycol are also suitable
for use as the additional nonionic surfactant systems of the present
invention.
The hydrophobic portion of these compounds will preferably have a molecular
weight of from about 1500 to about 1800 and will exhibit water insolubility.
The
addition of polyoxyethylene moieties to this hydrophobic portion tends to
increase the water solubility of the molecule as a whole, and the liquid
character
of the product is retained up to the point where the polyoxyethylene content
is
about 50% of the total weight of the condensation product, which corresponds
to
condensation with up to about 40 moles of ethylene oxide. Examples of
compounds of this type include certain of the comrn~;rcially-available
PlurafacTM
LF404 and PluronicTM surfactants, marketed by BA;iF.
Also suitable for use as the nonionic surfactant of the' nonionic surfactant
system
of the present invention, are the condensation proclucts of ethylene oxide
with
the product resulting from the reaction of propylene oxide and
ethylenediamine.
The hydrophobic moiety of these products consist:> of the reaction product of
ethylenediamine and excess propylene oxide, and generally has a molecular
weight of from about 2500 to about 3000. Tlhis hydrophobic moiety is
condensed with ethylene oxide to the extent that the condensation product
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26
contains from about 40% to about 80% by weight of polyoxyethylene and has a
molecular weight of from about 5,000 to about 11,~D00. Examples of this type
of
nonionic surfactant include certain of the commercially available TetronicTM
compounds, marketed by BASF.
Preferred for use as the nonionic surfactant of the surfactant systems of the
present invention are polyethylene oxide condensates of alkyl phenols,
condensation products of primary and secondary aliphatic alcohols with from
about 1 to about 25 moles of ethylerie oxide, alkylp~olysaccharides, and
mixtures
thereof. Most preferred are Cg-C14 alkyl phenol etlhoxylates having from 3 to
15
ethoxy groups and Cg-C1g alcohol ethoxylates (preferably C10 avg.) having
from 2 to 10 ethoxy groups, and mixtures thereof.
Highly preferred nonionic surfactants are polyhydroxy fatty acid amide
surfactants of the formula.
R2-C-N-Z,
O R1
wherein R1 is H, or R1 is C1_4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl
or
a mixture thereof, R2 is C5_31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyi
having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected
to
the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl, R2
is a
straight C11_15 alkyl or C1g_1g alkyl or aikenyl chain such as coconut alkyl
or
mixtures thereof, and Z is derived from a reducing sugar such as glucose,
fructose, maltose, lactose, in a reductive amination reaction.
Suitable anionic surfactants to be used are linear alkyl benzene sulfonate,
alkyl
ester sulfonate surfactants including linear esters of Cg-C20 carboxylic acids
(i.e., fatty acids) which are sulfonated with gaseous S03 according to "The
Journal of the American Oil Chemists Society°°, 52 (19?5), pp.
323-329. Suitable
starting materials would include natural fatty substances as derived from
tallow,
palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry
applications,
comprise alkyl ester sulfonate surfactants of the struictural formula:
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WO 99/57259 PCT/US99109409
27
O
I I
R3 - CH - C - OR4
I
S03M
wherein R3 is a Cg-C2p hydrocarbyl, preferably an alkyl, or combination
thereof,
R4 is a C1-C6 hydrocarbyl, preferably an alkyl, or combination thereof, and M
is
a ration which forms a water soluble salt with the alkyl ester sulfonate.
Suitable
salt-forming rations include metals such as sodium, potassium, and lithium,
and
substituted or unsubstituted ammonium rations, such as mono-ethanolamine,
diethanolarnine, and triethanolamine. Preferably, R3 is C10-C1g alkyl, and R4
is
methyl, ethyl or isopropyl. Especially preferred are the methyl ester
sulfonates
wherein R3 is C10-C1g alkyl.
Other suitable anionic surfactants include the alkyl sulfate surfactants which
are
water soluble salts or acids of the formula ROSO~sM wherein R preferably is a
C10-C24 hYdrocarbyl, preferably an alkyl or hydroxyalkyl having a C10-C20
alkyl
component, more preferably a C12-C18 alkyl or hydroxyalkyl, and M is H or a
ration, e.g., an alkali metal ration (e.g. sodium, potassium, lithium), or
ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl
ammonium rations and quaternary ammonium rations such as tetramethyl-
ammonium and dimethyl piperdinium rations and quaternary ammonium rations
derived from alkylamines such as ethylamine, diethylamine, triethylamine, and
mixtures thereof, and the like). Typically, alkyl chaiins of C12-C16 are
preferred
for lower wash temperatures (e.g. below about 50°C) and C16-18 alkyl
chains
are preferred for higher wash temperatures (e.g. above about 50°C).
Other anionic surfactants useful for detersive purposes can also be included
in
the laundry detergent andlor fabric care compositions of the present
invention.
These can include salts (including, for example, sodium, potassium, ammonium,
and substituted ammonium salts such as mono-, di-~ and triethanolamine salts)
of
soap, Cg-C22 primary of secondary alkanesulfonates, Cg-C24 olefinsulfonates,
sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed
product
of alkaline earth metal citrates, e.g., as described in British patent
specification
No. 1,082,179, Cg-C24 alkylpolyglycolethersulfates (containing up to 10 moles
of ethylene oxide); alkyl glycerol sulfonates, fatty ;aryl glycerol
sulfonates, fatty
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oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin
sulfonates, alkyl phosphates, isethionates such as the aryl isethionates, N-
aryl
taurates, alkyl succinarnates and sulfosuccinates, rnonoesters of
sulfosuccinates
(especially saturated and unsaturated C~2-C1g imonoesters) and diesters of
sulfosuccinates (especially saturated and unsatuirated Cg-C12 diesters), aryl
sarcosinates, sulfates of alkyipolysaccharides such as the sulfates of
alkylpolyglucoside (the nonionic nonsulfated compounds being described
below), branched primary alkyl sulfates, and alkyl polyethoxy carboxylates
such
as those of the formula RO(CH2CH20)k-CH2C0C)-M+ wherein R is a Cg-C22
alkyl, k is an integer from 1 to 10, and M is a soluble salt-forming ration.
Resin
acids and hydrogenated resin acids are also suitable, such as rosin,
hydrogenated rosin, and resin acids and hydrogenated resin acids present in or
derived from tall oil.
Further examples are described in °'Surface Active Agents and
Detergents" {Vol.
I and II by Schwartz, Perry and Berch). A variety of such surfactants are also
generally disclosed in U.S. Patent 3,929,678, is:>ued December 30, 1975 to
Laughiin, et al. at Column 23, line 58 through Column 29, line 23 (herein
incorporated by reference).
When included therein, the laundry detergent compositions of the present
invention typically comprise from about 1 % to about 40%, preferably from
about
3% to about 20% by weight of such anionic surfactants.
Highly preferred anionic surfactants include alkyl alkoxylated sulfate
surfactants
hereof are water soluble salts or acids of the formula RO(A)mS03M wherein R
is an unsubstituted C10-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl
component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-
C1g alkyl or hydroxyalkyl, A is an ethoxy or propox~~ unit, m is greater than
zero,
typically between about 0.5 and about 6, more preferably between about 0.5 and
about 3, and M is H or a ration which can be, for example, a metal ration
(e.g.,
sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or
substituted-ammonium ration. Alkyl ethoxylated sulfates as well as alkyl
propoxylated sulfates are contemplated herein. Specific examples of
substituted
ammonium rations include methyl-, dimethyl, trimc~thyl-ammonium rations and
quaternary ammonium rations such as tetramethyl-ammonium and dimethyl
piperdinium rations and those derived from alkyl:amines such as ethylamine,
CA 02331137 2000-10-31
WO 99/57259 PCTIUS99109409
29
diethylamine, triethylamine, mixtures thereof, and the like. Exemplary
surfactants
are C12-C18 alkyl polyethoxylate (1.0) sulfate (C12-CIgE{1.0)M), C12-C1g alkyl
polyethoxylate (2.25) sulfate (C12-C18E(2.25)M), (~12-C1g alkyl polyethoxylate
(3.0) sulfate (C12-C18E(3.0)M), and C12-C18 alkyl polyethoxylate (4.0) sulfate
(C12-C18E(4.0)M), wherein M is conveniently selected from sodium and
potassium.
The laundry detergent and/or fabric care compositiions of the present
invention
may also contain ampholytic, zwitterionic, and semi-polar surfactants, as well
as
the nonionic andlor anionic surfactants other than those already described
herein.
Ampholytic surfactants are also suitable for use in the laundry detergent
and/or
fabric care compositions of the present invention.. These surfactants can be
broadly described as aliphatic derivatives of secondary or tertiary amines, or
aliphatic derivatives of heterocyclic secondary and tertiary amines in which
the
aliphatic radical can be straight- or branched-chain. One of the aliphatic
substituents contains at least about 8 carbon atoms, typically from about 8 to
about 18 carbon atoms, and at least one contains an anionic water-solubilizing
group, e.g. carboxy, sulfonate, sulfate. See U.S. Patent No. 3;929,fi78 to
Laughlin et al., issued December 30, 1975 at ~;,olumn 19, lines 18-35, for
examples of ampholytic surfactants.
When included therein, the laundry detergent and/or fabric care compositions
of
the present invention typically comprise from 0.2'% to about 15%, preferably
from about 1 % to about 10% by weight of such amp~holytic surfactants.
Zwitterionic surfactants are also suitable for use in laundry detergent andlor
fabric care compositions. These surfactants can be broadly described as
derivatives of secondary and tertiary amines, derivatives of heterocyclic
secondary and tertiary amines, or derivatives of quaternary ammonium,
quaternary phosphonium or tertiary sulfonium compounds. See U.S. Patent No.
3,929,678 to Laughlin et al., issued December 30" 1975 at column 19, line 38
through column 22, line 48, for examples of zwitterioniG surfactants.
CA 02331137 2000-10-31
WO 99/57259 PCT/US99/09409
When included therein, the laundry detergent andlor fabric care compositions
of
the present invention typically comprise from 0.2;% to about 15%, preferably
from about 1% to about 10% by weight of such zwiiterionic surfactants.
Semi-polar nonionic surfactants are a special category of nonionic surfactants
which include water-soluble amine oxides containing one alkyl moiety of from
about 10 to about 18 carbon atoms and 2 moieties selected from the group
consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to
about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl
moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from
the group consisting of alkyl groups and hydroxyalkyl groups containing from
about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one
alkyl moiety of from about 10 to about 18 carbon .atoms and a moiety selected
from the group consisting of alkyl and hydroxyaikyl moieties of from about 1
to
about 3 carbon atoms.
Semi-polar nonionic detergent surfactants include the amine oxide surfactants
having the formula
0
T
R3(OR4)xN(R5)2
wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof
containing from about 8 to about 22 carbon ai:oms; R4 is an alkylene or
hydroxyalkylene group containing from about 2 to about 3 carbon at~ms or
mixtures thereof; x is from 0 to about 3; and each 1~5 is an alkyl or
hydroxyalkyl
group containing from about 1 to about 3 carbon atoms or a polyethylene oxide
group containing from about 1 to about 3 ethylene oxide groups. The R5 groups
can be attached to each other, e.g., through an oxygen or nitrogen atom, to
form
a ring structure.
These amine oxide surfactants in particular include C10-C1 g alkyl dimethyl
amine oxides and Cg-C12 alkoxy ethyl dihydroxy etl'~yl amine oxides.
When included therein, the cleaning compositions of the present invention
typically comprise from 0.2% to about 15%, preferably from about 1 % to about
10% by weight of such semi-polar nonionic surfactaints.
CA 02331137 2000-10-31
WO 99157259 PCTlUS99109409
31
The laundry detergent andlor fabric care composition of the present invention
may further comprise a cosurfactant selected from the group of primary or
tertiary amines.
Suitable primary amines for use herein include amiines according to the
formula
R1NH2 wherein R1 is a Cg-Cl2t preferably Cg-C1~~ alkyl chain or R4X(CH2~n, X
is -O-,-C(O)NH- or -NH-, Rq, is a Cg-C12 alkyl chain n is between 1 to 5,
preferably 3. R1 alkyl chains may be straight or branched and may be
interrupted with up to 12, preferably less than 5 ethylene oxide moieties.
Preferred amines according to the formula herein above are n-alkyl amines.
Suitable amines for use herein may be selected from 1-hexylamine, 1-
octylamine, 1-decylamine and laurylamine. Other preferred primary amines
include C8-C10 oxypropylamine, octyioxypropylamine, 2-ethylhexyloxypropyl-
amine, lauryl amido propylamine and amido propylaimine.
Suitable tertiary amines for use herein include tertiary amines having the
formula
R1 R2RgN wherein R1 and R2 are C1-Cg alkylchains or
Rs
-~ CHZ-CH-O~H
R~ is either a Cg-C12, preferably Cg-C1 p alkyl chain, or R3 is R4X(CH2)n,
whereby X is -O-, -C(O)NH- or -NH-,R4 is a C4-C129 n is between 1 to 5,
preferably 2-3. R~ is H or C1-C2 alkyl and x is between 1 to 6 .
R8 and R4 may be linear or branched ; Rg alkyl chains may be interrupted with
up to 12, preferably less than 5, ethylene oxide moieties.
Preferred tertiary amines are R1 R2R3N where R1 is a C6-C12 alkyl chain, R2
and R3 are C1-C3 alkyl or
Rs
1
-( CHZ-CH-O~H
where R5 is H or CH3 and x = 1-2.
Also preferred are the amidoamines of the formula:
CA 02331137 2000-10-31
WO 99/57259 PCT/US99/09~109
32
O
R1-C-NH-( CHZ n N-( R2 2
wherein R1 is Cg-C1~ alkyl; n is 2-4,
preferably n is 3; Rz and R3 is C1-C4
Most preferred amines of the present invention include 1-octylamine, 1-
hexylamine, 1-decylamine, 1-dodecylamine,CB-10oxypropylamine, N coco 1-
3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl
bis(hydroxyethyl)amine, coco bis(hydroxyehtyl}amine, lauryl amine 2 moles
propoxylated, octyl amine 2 moles propoxylated, lauryl arnidopropyl-
dimethylamine, C8-10 amidopropyldimethylamine and C10 amidopropyl-
dimethylamine.
The most preferred amines for use in the compositions herein are 1-hexyiamine,
1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n-
dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7
times ethoxylated, lauryi amido propylamine and cocoamido propylamine.
Conventional detergent enzymes
The laundry detergent and/or fabric care compositions can in addition to the
modified cellulase, further comprise one or mare enzymes which provide
cleaning performance andlor fabric care benefits.
Said other enzymes include enzymes selected fronn cellulases without naturally
occuring CSDs or with a having a relative binding constant (Kr-a) for binding
to
amorphous cellulose lower than 2.41/gcellulose, hemicellulases, peroxidases,
proteases, gluco-amylases, amylases, xylanase:>, lipases, phospholipases,
esterases, cutinases, pectinases, keratanase~s, reductases, oxidases,
phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases,
pentosanases, malanases, f3-glucanases, arabinosidases, hyaluronidase,
chondroitinase, laccase or mixtures thereof.
CA 02331137 2000-10-31
WO 99/57259 PCT/US99/09409
33
A preferred combination is a laundry detergent andlor fabric care composition
having cocktail of conventional applicable enzymes like protease, amylase,
lipase, cutinase and/or cellulase in conjunction with one or more plant cell
wall
degrading enzymes.
Suitable proteases are the subtilisins which are obtained from particular
strains
of B. subtilis and B. licheniformis (subtilisin BPIN and BPN'). One suitable
protease is obtained from a strain of Bacillus, having maximum activity
throughout the pH range of 8-12, developed and sold as ESPERASE~ by Novo
Industries AIS of Denmark, hereinafter "Novo". The preparation of this enzyme
and analogous enzymes is described in GB 1,243"784 to Novo. Other suitable
proteases include ALCALASE~, DURAZYM~ and SAVINASE~ from Novo and
MAXATASE~~ MAXACAL~, PROPERASE~ and MAXAPEM~ (protein
engineered Maxacal) from Gist-Brocades. Proteolytic enzymes also encompass
modified bacterial serine proteases, such as those described in European
Patent Application Serial Number 87 303761.8, filed April 28, 1987
(particularly
pages 17, 24 and 98), and which is called herein "Protease B", and in European
Patent Application 199,404, Venegas, published October 29, 1986, which refers
to a modified bacterial serine protealytic enzyme which is called "Protease A"
herein. Suitable is what is called herein "Protease; C", which is a variant of
an
alkaline serine protease from Bacillus in which lysine replaced arginine at
position 27, tyrosine replaced valine at position 104, serine replaced
asparagine
at position 123, and alanine replaced threonine ai: position 274. Protease C
is
described in EP 90915958:4, corresponding to WO 91106637, Published May
16, 1991. Genetically modified variants, particul<arly of Protease C, are also
included herein.
A preferred protease referred to as "Protease D" is a carbonyl hydrolase
variant
having an amino acid sequence not found in nature, which is derived from a
precursor carbonyl hydrolase by substituting a different amino acid for a
plurality
of amino acid residues at a position in said carbonyl hydrolase equivalent to
position +7fi, preferably also in combination with one or more amino acid
residue
positions equivalent to those selected from the group consisting of +99, +101,
+103, +104, +107, +123, +27, +105, +109, +126, +'i28, +135, +156, +166, +195,
+197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274
according to the numbering of Bacillus amyloliquefK~ciens subtilisin, as
described
in W095110591 and in the patent application of C. Ghosh, et al, "Bleaching
CA 02331137 2000-10-31
WO 99!57259 PCT/US99/09409
34
Compositians Comprising Protease Enzymes'° having US Serial No.
08/322,677,
filed October 13, 1994. Also suitable is a carbonyl hydrolase variant of the
protease described in W095i10591, having an amiino acid sequence derived by
replacement of a plurality of amino acid residues replaced in the precursor
enzyme corresponding to position +210 in combination with one or more of the
following residues : +33, +629 +67, +76, +100, +101, +103, +104, +107, +128,
+129, +130, +132, +135, +156, +158, +164, +16.6, +167, +170, +209, +215,
+217, +218, and +222, where the numbered position corresponds to naturally-
occurring subtilisin from Bacillus arriyloliquefaciens or to equivalent amino
acid
residues in other carbonyl hydrolases or subtiiisins, such as Bacillus lentos
subtilisin (ca-pending patent application US Serial No. 60/048,550, filed June
04,
1997).
Also preferred proteases are multiply-substituted! protease variants. These
protease variants comprise a substitution of an amino acid residue with
another
naturally occurring amino acid residue at an amino acid residue position
corresponding to position 103 of Bacillus arrryloliquefaciens subtilisin in
combination with a substitution of an amino acid re;>idue positions
corresponding
to positions 1, 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 1 !~, 20, 21, 22, 24, 27,
33, 37,
38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, T7, 78, 79, 86, 87, 89,
97, 98,
99, 101, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128,
130, 131, 133, 134, 137, 140, 141, 142, 146, 147, '158, 159, 160, 166, 167,
170,
173, 174, 177, 181, 182, 183, 184, 185, 188, 192, '194, 198, 203, 204, 205,
206,
209, 210, 211, 212, 213, 214, 215, 216, 217, 218, :?22, 224, 227, 228, 230,
232,
236, 237, 238, 240, 242, 243, 244, 245, 246, 247, :?48, 249, 251, 252, 253,
254, ,
255, 256, 257, 258, 259, 260, 261, 262, 263, 265, .268, 269, 270, 271, 272,
274
and 275 of Bacillus amyloliquefaciens subtilisin; wherein when said protease
variant includes a substitution of amino acid residues at positions
corresponding
to positions 103 and 76, there is also a substitution of an amino acid residue
at
one or more amino acid residue positions othE:r than amino acid residue
positions corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128,
166,
204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus
amyloliquefaciens subtiiisin and/or multiply-substituted protease variants
comprising a substitution of an amino acid re:;idue with another naturally
occurring amino acid residue at one or more amino acid residue positions
corresponding to positions 62, 212, 230, 232, 252 and 257 of Bacillus
amyloliquefaciens subtilisin as described in PCT application Nos.
CA 02331137 2000-10-31
WO 99157259 PCT/US99109409
PCTIUS98122588, PCT/US98/22482 and PCTIUS!38/22486 all filed on October
23, 1998 from The Procter & Gamble Company.
Also suitable for the present invention are proteases described in patent
applications EP 251 446 and WO 91 /06637, protease BLAP~ described in
W091/02792 and their variants described in WO 9;i/23221.
See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO
93118140 A to Novo. Enzymatic detergents comprising protease, one or more
other enzymes, and a reversible protease inhiibitor are described in WO
92103529 A to Novo. When desired, a protease having decreased adsorption
and increased hydrolysis is available as described in WO 95/07791 to Procter ~
Gamble. A recombinant trypsin-like protease for detergents suitable herein is
described in WO 94/25583 to Novo. Other suitable proteases are described in
EP 516 200 by Unilever.
The proteolytic enzymes are incorporated in the eletergent compositions of the
present invention a level of from 0.0001 % to 2°/«, preferably from
0:001 % to
0.2%, more preferably from 0.005% to 0.1 % pure enzyme by weight of the
composition.
The cellulases without naturally occurring CBDs or with a having a relative
binding constant (Kr-a) for binding to amorphous cellulose lower than
2.411gcellulose, include both bacterial or fungal ce~llulases. Preferably,
they will
have a pH optimum of between 5 and 72 and an activity above 50 CEVU
(Cellulose Viscosity Unit). Suitable cellulases acre disclosed in U.S. Patent
4,435,307, Barbesgoard et al, J61078384 and VV096/02653 which discloses
fungal cellulase produced respectively from Hurrricofa insolens, Trichoderma,
Thielavia and Sporotrichum. EP 739 982 describes cellulases isolated from
novel Bacillus species. Suitable cellulases arE: also disclosed in GB-A-
2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and W095I26398.
Examples of such cellulases are cellulases produced by a strain of Humicola
insolens (Humicofa grisea var. thermoidea), particularly the Humicola strain
DSM
1800. Other suitable celluiases are cellulases originated from Humicola
insolens
having a molecular weight of about 50KDa, an isoelectric point of 5.5 and
containing 415 amino acids; and a -43kD endoglucanase derived from Humicola
insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase
component has the amino acid sequence disclosed in PCT Patent Application
CA 02331137 2000-10-31
WO 99/57259 PCT/IJS99/09409
36
No. WO 91!17243. Also suitable cellulases are the EGIII cellulases from
Trichoderma longibrachiatum described in W094l21801, Genencor, published
September 29, 1994. Especially suitable cellulases are the cellulases having
color care benefits. Examples of such cellulases; are cellulases described in
European patent application No. 91202879.2, filed November fi, 1991 (Novo).
Carezyme and Celluzyme (Novo Nordisk A/S) arcs especially useful. See also
W091117244 and W091/21801. Other suitable cellulases for fabric care and/or
cleaning properties are described in W096~I34092, W096l17994 and
W095/24471.
Said cellulases are normally incorporated in the df;tergent composition at
levels
from 0.0001 % to 2% of pure enzyme by weight of the detergent composition.
Peroxidase enzymes are used in combination with oxygen sources, e.g.
percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a
phenolic
substrate as bleach enhancing molecule. They are used for "solution
bleaching",
i.e. to prevent transfer of dyes or pigments removed from substrates during
wash operations to other substrates in the wash solution. Peroxidase enzymes
are known in the art, and include, for example, horseradish peroxidase,
ligninase
and haioperoxidase such as chloro- and bromo-peroxidase. Peroxidase-
containing detergent compositions are disclosed, for example, in PCT
International Application WO 89/099813, W089!09813 and in European Patent
application EP No. 91202882.f>, filed on November 6, 1991 and EP No.
96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme.
Enhancers are generally comprised at a level of from 0.1 % to 5% by weight of
total composition. Preferred enhancers are substituted phenthiazine and
phenoxasine 10-Phenothiazinepropionicacid {PPT), 10-ethylphenothiazine-4-
carboxyfic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-
methylphenoxazine (described in WO 94112621) and substituted syringates (C3-
C5 substituted alkyl syringates) and phenols. Sodium percarbonate or perborate
are preferred sources of hydrogen peroxide.
Said peroxidases are normally incorporated in the detergent composition at
levels from 0.0001 % to 2°/~ of pure enzyme by weight of the detergent
composition.
Other enzymes that can be included in the detergent compositions of the
present invention include lipases. Suitable lipase enzymes for detergent usage
CA 02331137 2000-10-31
WO 99/57259 ° PCT/(JS99109409
37
include those produced by microorganisms of the Pseudomonas group, such as
Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034.
Suitable lipases include those which show a positive immunological cross-
reaction with the antibody of the lipase, produced by the microorganism
Pseudomonas fluorescent IAM 1057. This lipase is available from Amano
Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P
"Amano," hereinafter referred to as "Amano-P". Other suitable commercial
lipases include Amano-CES, lipases ex Ch!romobacter viscosum, e.g.
Chromobacfer viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co.,
Tagata, Japan; Chromobacter viscosum lipases i'rom U.S. Biochemical Corp.,
U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas
gladioli. Especially suitable lipases are lipases such as M1 LipaseR and
LipomaxR (Gist-Brocades) and LipolaseR and lLipolase UItraR(Novo) which
have found to be very effective when used in combination with the compositions
of the present invention. Also suitables are the lipollytic enzymes described
in EP
258 068, WO 92105249 and WO 95122615 by Novo Nordisk and in WO
94/03578, WO 95135381 and WO 96/00292 by Unilever.
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special
kind of lipase, namely lipases which do not require interfacial activation.
Addition
of cutinases to detergent compositions have been described in e.g. WO-A-
88109367 (Genencor}; WO 90109446 {Plant Genetic System) 'and WO 94/14963
and WO 94/14964 (Unilever).
The lipases and/or cutinases are normally incorporated in the detergent
composition at levels from 0.0001 % to 2% of pure enzyme by weight of the
detergent composition.
Amylases (oc and/or (3) can be included for removal of carbohydrate-based
stains. W094/02597, Novo Nordisk A/S published February 03, 1994, describes
cleaning compositions which incorporate mutant amylases. See also
W095/10603, Novo Nordisk AIS, published April 20, 1995. Other amylases
known for use in cleaning compositions include both a- and [i-amylases. a,-
Amylases are known in the art and include tho;>e disclosed in US Pat. no.
5,003,257; EP 252,666; W0/91/00353; FR 2,676,456; EP 285,123; EP 525,610;
EP 368,341; and British Patent specification n~o. 1,296,839 (Novo}. Other
suitable amylases are stability-enhanced amylasea described in W094I18314,
published August 18, 1994 and W096/05295, Genencor, published February
CA 02331137 2000-10-31
WO 99!57259 PCT/US99/09409
38
. 22, 1996 and amylase variants having additional modification in the
immediate
parent available from Novo Nordisk A/S, disclosed in WO 95/10f03, published
April 95. Also suitable are amylases described in EP 277 216, W095/26397
and W096/23873 (all by Novo Nordisk).
Examples of commercial a-amylases products are Purafect Ox Am~ from
Genencor and Termamyl~, Ban~ ,Fungamyl~ and Durarnyl~, all available from
Novo. Nordisk AIS Denmark. W095/26397 describfa other suitable amylases : a
-amylases characterised by having a specific activity at least 25% higher than
the specific activity of Termamyl~ at a temperature range of 25°C to
55°C and
at a pH value in the range of 8 to 10, measured b~y the Phadebas~ a-amylase
activity assay. Suitable are variants of the above enzymes, described in
W096/23873 (Novo Nordisk). Other amylolytic enzymes with improved
properties with respect to the activity level and the combination of
thermostability
and a higher activity level are described in W095/35382.
The amylolytic enzymes are incorporated in the detergent compositions of the
present invention a level of from 0.0001 % to 2%, preferably from 0.00018% to
0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the
composition.
The above-mentioned enzymes may be of any suitable origin, such as
vegetable, animal, bacterial, fungal and yeast origin. Origin can further be
mesophilic or extremophilic (psychrophilic, p;sychrotrophic, thermophilic,
barophilic, alkalophilic, acidophilic; halophilic, etc.). Purified or non-
purified forms
of these enzymes may be used. Also included by definition, are mutants of
native enzymes. Mutants can be obtained e.g. by protein and/or genetic
engineering, chemical and/or physical modifications of native enzymes.
Common practice as well is the expression of the enzyme via host organisms in
which the genetic material responsible for the production of the enzyme has
been cloned.
Said enzymes are normally incorporated in the detergent composition at levels
from 0.0001 % to 2% of pure enzyme by weight oiF the detergent composition.
The enzymes can be added as separate single ingredients (prills, granulates,
stabilized liquids, etc. containing one enzyme ) or as mixtures of two or more
enzymes ( e.g. cogranulates ).
CA 02331137 2000-10-31
WO 99157259 PCT/I1S99/09409
39
Other suitable detergent ingredients that can be added are enzyme oxidation
scavengers which are described in Copending European Patent application
92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation
scavengers are ethoxylated tetraethylene polyamines.
A range of enzyme materials and means for their incorporation into synthetic
detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A
to Genencor International, WO 8908694 A to Novo, and U.S. 3,553,139,
January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S.
4,101,457, Place et al; July 18, 1978, and in U.S. 4,507,219, Hughes, March
26,
1985. Enzyme materials useful for liquid detergent formulations, and their
incorporation into such formulations, are disclosed in U.S. 4,261,868, Hora et
al,
April 14, 1981. Enzymes for use in detergents can be stabilised by various
techniques. Enzyme stabilisation techniques are disclosed and exemplified in
U.S. 3,600,319, August 17, 1971, Gedge et al, E:P 199,405 and EP 200,586,
October 29, 1986, Venegas. Enzyme stabilisation systems are also described,
for example, in U.S. 3,519,570. A useful Bacillus>, sp. AC13 giving proteases,
xylanases and cellulases, is described in WO 9401:532 A to Novo.
Colour care and fabric care benefits
Technologies which provide a type of colour care benefit can also be included.
Examples of these technologies are metallo catalysts for colour maintenance.
Such metallo catalysts are described in copending European Patent Application
No. 92870181.2. Dye fixing agents, polyolefin dispersion for anti-wrinkles and
improved water absorbancy, perfume and amino-functional polymer for color
care treatment and perfume substantivity are further examples of colour care I
fabric care technologies and are described in the co-pending Patent
Application
No. 96870140.9, filed November 07, 1996.
Fabric softening agents can also be incorporated unto laundry detergent and/or
fabric care compositions in accordance with the present invention. These
agents
may be inorganic or organic in type. Inorganic softening agents are
exemplified
by the smectite clays disclosed in GB-A-1 400 898 and in USP 5,019,292.
Organic fabric softening agents include the water insoluble tertiary amines as
disclosed in GB-A1 514 276 and EP-BO 011 340 and their combination with
CA 02331137 2000-10-31
WO 99157259 PCT/U599/09409
mono C12-C14 quaternary ammonium salts are disclosed in EP-B-0 026 527
and EP-B-0 026 528 and di-long-chain amides as disclosed in EP-B-0 242 919.
Other useful organic ingredients of fabric softening systems include high
molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575
and 0 313 146.
Preferred fabric softening agent for the purpose of the present invention is a
smectite clay. It has been surprisingly found that the laundry detergent
and/or
fabric care compositions of the present invention further comprising a
smectite
clay, achieve improved fabric care, including improved anti-wrinkle, anti-
bobbling
and anti-shrinkage properties to fabrics, as well as provide enhanced static
control, fabric softness, colour appearance and fabric anti-wear properties
and
benefits while preventing tensile strength loss.
Levels of smectite clay are normally in the range from 2% to 20%, more
preferably from 5% to 15% by weight, with the material being added as a dry ,
mixed component to the remainder of the formulation. Organic fabric softening
agents such as the water-insoluble tertiary amiines or dilong chain amide
materials are incorporated at levels of from 0.5% to 5% by weight, normally
from
1 % to 3% by weight whilst the high molecular weight polyethylene oxide
materials and the water soluble cationic materials are added at levels of from
0.1 % to 2%, normally from 0.15% to 1.5% by weight. These materials are
normally added to the spray dried portion of the composition, although in some
instances it may be more convenient to add them as a dry mixed particulate, or
spray them as molten liquid on to other solid components of the composition.
Bleaching agent
Other detergent ingredients that can be included in the laundry detergent
and/or
fabric care compositions of the present invention include bleaching agents.
Bleaching agents include hydrogen peroxide, PB1, I'B4 and percarbonate with a
particle size of 400-800 microns. These bleaching agent components can
include one or more oxygen bleaching agents and, depending upon the
bleaching agent chosen, one or more bleach activsitors. When present oxygen
bleaching compounds will typically be present at levels of from about 1 % to
about 25%.
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WO 99l57Z59 PCT/US99/09409
41
The bleaching agent component for use herein c:an be any of the bleaching
agents useful for cleaning compositions including oxygen bleaches as well as
others known in the art. The bleaching agent suitable for the present
invention
can be an activated or non-activated bleaching agent.
One category of oxygen bleaching agent that can be used encompasses
percarboxylic acid bleaching agents and salts therE:of. Suitable examples of
this
class of agents include magnesiuim monoperox~yphthalate hexahydrate, the
magnesium salt of meta-chioro perbenzoic acid, 4-nonylamino-4-
oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents
are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446,
European Patent Application 0,133,354 and U.;i. Patent 4,412,934. Highly
preferred bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid
as described in U.S. Patent 4,634,551.
Another category of bleaching agents that can be used encompasses the
halogen bleaching agents. Examples of hypohalite bleaching agents, for
example; include trichloro isocyanuric acid and the sodium and potassium
dichloroisocyanurates and N-chloro and N-bromo <~Ikane sulphonamides. Such
materials are normally added at 0.5-10% by weight of the finished product,
preferably 1-5% by weight.
The hydrogen peroxide releasing agents can be usE:d in combination with bleach
activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-
sulfonate (HOBS, described in I.IS 4,412,934), 3,5,-
trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or
pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-
aminocaproic acid (NAOA-OBS, described in WO94/28106), which are
perhydrolyzed to form a peracid as the active bleaching species, leading to
improved bleaching effect. Also suitable activators are acylated citrate
esters
such as disclosed in Copending European Patent Application No. 91870207.7.
Useful bleaching agents, including peroxyacids and bleaching systems
comprising bleach activators and peroxygen bfeac;hing compounds for use in
detergent compositions according to the inventioin are described in our co-
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92
pending, applications USSN 08/136,626, PCl-IUS95/07823, W095/27772,
WO95/27773, W095127774 and W095I27775.
The hydrogen peroxide may also be present by adding an enzymatic system
(i.e., an enzyme and a substrate therefore) which is capable of generating
hydrogen peroxide at the beginning or during the washing andlor rinsing
process. Such enzymatic systems are disclosed in EP Patent Application
91202655.6 fled October 9, 1991.
Metal-containing catalysts for use in bleach compositions, include cobalt-
containing catalysts such as Pentaamine acetate cobalt(III) salts and
manganese-containing catalysts such as those described in EPA 549 271; EPA
549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US
5,114,611. Bleaching composition comprising a pecoxy compound, a
manganese-containing bleach catalyst and a chelating agent is described in the
patent application No 94870206.3.
Bleaching agents other than oxygen bleaching agents are also known in the art
and can be utilized herein. One type of non-oxygen bleaching agent of
particular
interest includes photoactivated bleaching agents such as the sulfonated zinc
and/or aluminum phthalocyanines. These materials can be deposited upon the
substrate during the washing process. Upon ilrradiation with light, in the
presence of oxygen, such as by hanging clothes out to dry in the daylight, the
sulfonated zinc phthalocyanine is activated and, consequently, the substrate
is
bleached. Preferred zinc phthalocyanine and .a photoactivated bleaching
process are described in U.S. Patent 4,033,7'18. Typically, detergent
compositions wile contain about 0.025% to about 1.25%, by weight, of
suifonated
zinc phthalocyanine.
Builder system
The compositions according to the present invention may further comprise a
builder system. It has been surprisingly found that said laundry detergent
andlor
fabric care compositions further comprising a builcler, achieve improved
fabric
care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage
properties
to fabrics, as well as provide enhanced static control, fabric softness,
colour
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WO 99IS7259 PCT/US99/09409
43
appearance arid fabric anti-wear properties and benefits and improved fabric
cleaning while preventing tensile strength loss. Preferred builders are
zeolite A
and sodium tripolyphosphate.
Any conventional builder system is suitable for use herein including
aluminosiiicate materials, silicates, polycarboxylaires, alkyl- or alkenyl-
succinic
acid and fatty acids, materials such as ethylenediamine tetraacetate,
diethylene
triamine pentamethyleneacetate, metal ion sequ~estrants such as aminopoly-
phosphonates, particularly ethylenediamine tetramethylene phosphonic acid and
diethylene triamine pentamethylenephosphonic acid. Phosphate builders can
also be used herein.
Suitable builders can be an inorganic ion exchange material, commonly an
inorganic hydrated aluminosilicate material, more particularly a hydrated
synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered silicate, e.g. SKS-6
(Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium
silicate
(Na2Si205).
Suitable poiycarboxylates containing one carboxy group include lactic acid,
glycolic acid and ether derivatives thereof as discllosed in Belgian Patent
Nos.
831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups
include the water-soluble salts of succinic acid, rnalonic acid,
(ethylenedioxy)
diacetic acid, malefic acid, diglycollic acid, tartaric acid, tartronic acid
and fumaric
acid, as well as the ether carboxylates described in German Offenlegenschrift
2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and the suifinyl
carboxylates described in Belgian Patent No. 840,623. Polycarboxylates
containing three carboxy groups include, in particulbr, water-soluble
citrates,
aconitrates and citraconates as well as succinaite derivatives such as the
carboxymethyloxysuccinates described in British Patent No. 1,379,241,
lactoxysuccinates described in Netherlands Application 7205873, and the
oxypolycarboxylate materials such as 2-oxa-1,1,3-propane tricarboxylates
described in British Patent No. 1,387,447.
Polycarboxylates containing four carboxy groups include oxydisuccinates
disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates,
1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxylates.
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44
Polycarboxylates containing sulfo substituents include the sulfosuccinate
derivatives disclosed in British Patent Nos. 1,398,~121 and 1,398,422 and in
U.S.
Patent No. 3,936,448, and the sulfonated pyrolysed citrates described in
British
Patent No. 1,082,179, while polycarboxylates containing phosphone
substituents are disclosed in British Patent No. 1,439,000.
Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,cis,cis-
tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-
furan
- cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-~furan -cis -
dicarboxylates,
2,2,5,5-tetrahydrofuran - tetracarboxyiates, 1,2,3,4,5,6-hexane -hexa-
carboxylates and and carboxymethyl derivatives of polyhydric alcohols such as
sorbitol, mannitol and xylitol. Aromatic poly-carboxylates include mellitic
acid,
pyromellitic acid and the phthalic acid derivatives disclosed in British
Patent No.
1,425,343.
Of the above, the preferred polycarboxylates are hydroxycarboxylates
containing
up to three carboxy groups per molecule, more particularly citrates.
Preferred builder systems for use in the present compositions include a
mixture
of a water-insoluble aluminosilicate builder such as zeolite A or of a layered
silicate (SKS-6), and a water-soluble carboxylate chelating agent such as
citric
acid.
Preferred builder systems include a mixture of a wrater-insoluble
aluminosilicate
builder such as zeolite A, and a watersolubte carboxylate chelating agent such
as citric acid. Preferred builder systems for use in liquid detergent
compositions
of the present invention are soaps and polycarboxylates.
Other builder materials that can form part of the builder system for use in
granular compositions include inorganic materials such as alkali metal
carbonates, bicarbonates, silicates, and organic materials such as the organic
phosphonates, amino polyalkylene phosphonates and amino polycarboxylates.
Other suitable water-soluble organic salts are the homo- or co-polymeric acids
or their salts, in which the polycarboxylic acid comprises at least two
carboxyl
radicals separated from each other by not more than two carbon atoms.
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WO 99/57259 PCT/US99/09409
Polymers of this type are disclosed in GB-A-1,59Ei,756. Examples of such salts
are polyacrylates of MW 2000-5000 and their copolymers with malefic anhydride,
such copolymers having a molecular weight of from 20,000 to 70,000, especially
about 40,000.
Detergency builder salts are normally included in amounts of from 5% to 80% by
weight of the composition preferably from 10% to 70% and most usually from
30% to fi0% by weight.
Chelating Agents
The laundry detergent andlor fabric care compositions herein may also
optionally contain one or more iron and/or manganese chelating agents. Such
chelating agents can be selected from the group consisting of amino
carboxylates, amino phosphonates, polyfunctionally-substituted aromatic
chelating agents and mixtures therein, all as hereinafter defined. Without
intending to be bound by theory, it is believed that the benefit of these
materials
is due in part to their exceptional ability to remove iron and manganese ions
from washing solutions by formation of soluble chelates.
Amino carboxylates useful as optional chelating agents include
ethylenediaminetetracetates, N-hydroxyethyfethylf:nediaminetriacetates,
nitrilo-
triacetates, ethylenediamine tetraproprionaites, triethylenetetraamine-
hexacetates, diethylenetriaminepentaacetates, and ethanoldiglycines, alkali
metal, ammonium, and substituted ammonium salts therein and mixtures
therein.
Amino phosphonates are also suitable for use as chelating agents in the
compositions of the invention when at Lease low levels of total phosphorus are
permitted in detergent compositions, and include ethylenediaminetetrakis
(methylenephosphonates) as DEQUEST. Preferrec#, these amino phosphonates
do not contain alkyl or alkenyl groups with more than about 6 carbon atoms:
PoPyfunctionally-substituted aromatic chelating agents are also useful in the
compositions herein. See U.S. Patent 3,812,044'., issued May 21, 1974, to
Connor et a!. Preferred compounds of this type in acid form are
dihydroxydisulfobenzenes such as 1,2-dihydroxy-3,;5-disulfobenzene.
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WO 99/57259 PCT/US99/09409
46
A preferred biodegradable chelator for use herein is ethylenediamine
disuccinate ("EDDS"), especially the [S,S] isomer as described in U.S. Patent
4,704,233, November 3, 1987, to Hartman and Perkins.
The compositions herein may also contain water-soluble methyl glycine diacetic
acid (MGDA) salts (or acid form) as a chelant or co-builder useful with, for
example, insoluble builders such as zeolites, IayerE~d silicates and the like.
If utilized, these chelating agents will generally comprise from about 0.1 %
to
about 15% by weight of the detergent compositions herein. More preferably, if
utilized, the chelating agents will comprise from about 0.1 % to about 3.0% by
weight of such compositions.
Suds suppressor
Another optional ingredient is a suds suppressor, exemplified by silicones,
and
silica-silicone mixtures. Silicones can be generally represented by alkylated
polysiloxane materials while silica is normally wised in finely divided forms
exemplified by silica aerogels and xerogels and hydrophobic silicas of various
types. These materials can be incorporated as p<srticulates in which the suds
suppressor is advantageously releasably incorporated in a water-soluble or
water-dispersible, substantially non-surface-active detergent impermeable
carrier. Alternatively the suds suppressor can be dissolved or dispersed in a
liquid carrier and applied by spraying on to ~one or more of the other
components.
A preferred silicone suds controlling agent is disclosed in Bartoilota et al.
U.S.
Patent 3 933 672. Other particularly useful such suppressors are the self
emulsifying silicone suds suppressors, described in German Patent Application
DTOS 2 646 12fi published April 28, 1977. An example of such a compound is
DC-544, commercially available from Dow Corning, which is a siloxane-glycol
copolymer. Especially preferred suds controlling agent are the suds suppressor
system comprising a mixture of silicone oils and 2-alkyl-alcanols. Suitable 2-
alkyl-alkanols are 2-butyl-octanol which are commercially available under the
trade name Isofol 12 R.
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47
Such suds suppressor system are described in Copending European Patens
application N 92870174.7 filed 10 November, 199:?.
Especially preferred silicone suds controlling agents are described in
Copending
European Patent application N°92201649.8. Said compositions can
comprise a
silicone/silica mixture in combination with fumed nonporous silica such as
AerosilR.
The suds suppressors described above are normally employed at levels of from
0.001 % to 2% by weight of the composition, preferably from 0.01 % to 1 % by
weight.
Others
Other components such as soil-suspending ageni;s, soil-release agents, optical
brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents,
and/or.
encapsulated or non-encapsulated perfumes may be employed.
Especially suitable encapsulating materials are vuater soluble capsules which
consist of a matrix of polysaccharide and polyhydroxy compounds such as
described in GB 1,464,fi16.
Other suitable water soluble encapsulating materials comprise dextrins derived
from ungelatinized starch acid-esters of substituted dicarboxylic acids such
as
described in US 3,455,838. These acid-ester dextrins are,preferably, prepared
Pram such starches as waxy maize, waxy sorghum, sago, tapioca and potato.
Suitable examples of said encapsulating materials include N-Lok manufactured
by National Starch. The N-Lok encapsulating maiterial consists of a modified
maize starch and glucose. The starch is modified by adding monafunctional
substituted groups such as octenyl succinic acid anhydride.
Antiredeposition and soil suspension agents suitable herein include cellulose
derivatives such as methylcellulose, carboxymethylcellulose and
hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their
salts. Polymers of this type include the polyacryiates and malefic anhydride-
acrylic acid copolymers previously mentioned as builders, as well as
copolymers
of malefic anhydride with ethylene, methylvinyl ether or methacrylic acid, the
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WO 99/57259 PCT/t1S99/09409
48
malefic anhydride constituting at least 20 mole percent of the copolymer.
These
materials are normally used at levels of from 0.5% to 10% by weight, more
preferably from 0.75% to 8%, most preferably from 1 % to 6% by weight of the
composition.
Preferred optical brighteners are anionic in character, examples of which are
disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-
2:2'
disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino-
stilbene-2:2° - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-
triazin-6-
ylamino)stilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-
tri-
azin-6 ylamino)stilbene-2-sulphonate, disodium 4,~4' -bis-(2-anilino-4-(N-
methyl-
N-2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2' - disulphonate, di-
sodium 4,4' -bis-(4-phenyl-2,1,3-triazol-2-yl)-stilberne-2,2' disulphonate, di-
so-
dium 4,4'bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-6- ylami-
no)stilbene-2,2'disulphonate, sodium 2(stilbyl-4"-(naphtho-1',2':4,5)-1,2,3 -
triazole-2"-sulphonate and 4,4'-bis(2-sulphostyryll)biphenyl. Highly preferred
brighteners are the specific brighteners of copending European Patent
application No. 95201943.8.
Other useful polymeric materials are the polyethylene glycols, particularly
those
of molecular weight 1000-10000, more particularly 2000 to 8000 and most
preferably about 4000. These are used at levels of from 0.20% to 5% more
preferably from 0.25% to 2.5% by weight. These polymers and the previously
mentioned homo- or co-polymeric polycarboxyl;ate salts are valuable for
improving whiteness maintenance, fabric ash deposition, and cleaning
performance on clay, proteinaceous and oxidizat~le soils in the presence of
transition metal impurities.
Soil release agents useful in compositions of the present invention are
conventionally copolymers or terpolymers of tere~phthalic acid with ethylene
glycol andlor propylene glycol units in various arrangements. Examples of such
polymers are disclosed in the commonly assigned l1S Patent Nos. 4116885 and
4711730 and European Published Patent Application No. 0 272 033. A
particular preferred polymer in accordance with EP-I~-0 272 033 has the
formula
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WO 99/57259 PCT/fJS99109409
49
(CH3(PEG)43)0.75(POH)0,25~T-PO)2.g(T-PEG)0.4)T(PO
H)0.25((PEG)43CH3)0.75
where PEG is -(OC2H4)O-,PO is (OC3Hg0) and T is (pcOCgH4CO).
Also very useful are modified polyesters as random copolymers of dimethyl
terephthalate, dimethyl sulfoisophthaiate, ethylene glycol and 1-2 propane
diol,
the end groups consisting primarily of sulphobenzo~ate and secondarily of mono
esters of ethylene glycol and/or propane-diol. The target is to obtain a
polymer
capped at both end by sulphobenzoate groups, "primarily", in the present
context most of said copolymers herein will be end-capped by sulphobenzoate
groups. However, some copolymers will be less than fully capped, and therefore
their end groups may consist of monoester of ethylene glycol andlor propane 1-
2 diol, thereof consist "secondarily" of such species.
The selected polyesters herein contain about 4.fi% by weight of dimethyl
terephthalic acid, about 16% by weight of propane -1.2 diol, about 10% by
weight ethylene glycol about 13% by weight of dimethyl sulfobenzoic acid and
about 15% by weight of sulfoisophthalic acid, and have a molecular weight of
about 3.000. The polyesters and their method of preparation are described in
detail in EPA 311 342.
It is well known in the art that free chlorine in tap vvater rapidly
deactivates the
enzymes comprised in detergent compositions. Therefore, using chlorine
scavenger such as perborate, ammonium sulfate, sodium sulphite or
polyethyleneimine at a level above 0.1 % by weighs; of total composition, in
the
formulas will provide improved through the wash stability of the detergent
enzymes. Compositions comprising chlorine scavE:nger are described in the
European patent application 92870018.6 filed January 31, 1992.
Alkoxylated polycarboxylates such as those prepared from polyacrylates are
useful herein to provide additional grease removal p~erFormance. Such
materials
are described in WO 91/08281 and PCT 90/01815 .at p. 4 et sep., incorporated
herein by reference. Chemically, these materials comprise polyacrylates having
one ethoxy side-chain per every 7-8 acrylate units. The side-chains are of the
formula -(CH2CH20)m(CH2)nCH3 wherein m is 2-3 and n is 6-12. The side-
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WO 99/57259 PCT/~IS99/09409
chains are ester-linked to the poiyacrylate "backbone" to provide a "comb"
polymer type structure. The molecular weight can vary, but is typically in the
range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can
comprise from about 0.05% to about 10%, by weight, of the compositions
herein.
Dispersanfs
The laundry detergent and/or fabric care composition of the present invention
can also contain dispersants : Suitable water-soluble organic salts are the
homo-
or co-polymeric acids or their salts, in which the polycarboxylic acid
comprises at
least two carboxyl radicals separated from each .other by not more than two
carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts
are polyacrylates of MW 2000-5000 and their copolymers with malefic anhydride,
such copolymers having a molecular weight of from.1,000 to 100,000.
Especially, copolymer of acrylate and methyiacrylatE: such as the 480N having
a
molecular weight of 4000, at a level from 0.5-20% by weight of composition can
be added in the laundry detergent and/or fabric care compositions of the
present
invention.
The compositions of the invention may contain a lime soap peptiser compound,
which has preferably a lime soap dispersing power (LSDP), as defined
hereinafter of no more than 8, preferably no more than 7, most preferably no
more than 6. The lime soap peptiser compound is preferably present at a level
from 0% to 20% by weight.
A numerical measure of the effectiveness of a lime soap peptiser is given by
the
lime soap dispersant power (LSDP) which is determined using the lime soap
dispersant test as described in an article by H.C. Borghetty and C.A. Bergman,
J. Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime soap
dispersion test method is widely used by practitioners in this art field being
referred to, for example, in the following review articles; W.N. Linfield,
Surtactant
science Series, Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume
27,
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51
pages 159-163, (1990); and M.K. Nagarajan, VU.F. Master, Cosmetics and
Toiletries, volume 104, pages 71-73, (1989). The L.SDP is the % weight ratio
of
dispersing agent to sodium oleate required to disperse the lime soap deposits
formed by 0.025g of, sodium oleate in 30m1 of water of 333ppm CaCo3
(Ca:Mg=3:2) equivalent hardness.
Surtactants having good lime soap peptiser capability will include certain
amine
oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated
alcohols.
Exemplary surfactants having a LSDP of no more lrhan 8 for use in accord with
the present invention include C1g-C18 dimethyl <~mine oxide, C12-C1g alkyl
ethoxysulfates with an average degree of ethoxyla~tion of from 1-5,
particularly
C12-C15 alkyl ethoxysulfate surfactant with a degree of ethoxyfation of amount
3 (LSDP=4), and the C14-C15 ethoxylated alcohol:, with an average degree of
ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol
A012 and Lutensol A030 respectively, by BASF GmIbH.
Polymeric lime soap peptisers suitable for use hereon are described in the
article
by M.K. Nagat-ajan, W.F. Master, to be found in Cosmetics and Toiletries,
volume 104, pages 71-73, (1989).
Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyl]benzene
sulfonate, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl-6-
aminohexanoyl]benzene sulfonate and mixtures i;hereof; and nonanoyloxy
benzene sulfonate together with hydrophilic / hydrophobic bleach formulations
can also be used as lime soap peptisers compounds.
Dye transfer inhibition
The laundry detergent and/or fabric care compositions of the present invention
can preferably include compounds for inhibiting dye transfer from one fabric
to
another of solubilized and suspended dyes encountered during fabric laundering
operations involving colored fabrics. It has been surprisingly found that the
laundry detergent andlor fabric care compositions of the present invention
further comprising a dye transfer inhibition polymer, achieve improved fabric
care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage
properties
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WO 99!57259 PCT/US99/09409
52
to fabrics, as well as provide enhanced static c:ontrol, fabric softness,
colour
appearance and fabric anti-wear properties and benefits and improved fabric
cleaning while preventing tensile strength loss.
Polymeric dye transfer inhibiting agents
The laundry detergent andlor fabric care compositions according to the present
invention may also comprise from 0.001 % to 10 %., preferably from 0.01 % to
2%,
more preferably from 0.05% to 1 % by weight of polymeric dye transfer
inhibiting
agents. Said polymeric dye transfer inhibiting agents are normally
incorporated
into cleaning compositions in order to inhibit the transfer of dyes from
colored
fabrics onto fabrics washed therewith. These polymers have the ability to
complex or adsorb the fugitive dyes washed out o1F dyed fabrics before the
dyes
have the opportunity to become attached to other airticles in the wash.
Especially suitable polymeric dye transfer inhibiting agents are polyamine N-
oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole,
polyvinylpyrrolidone polymers, polyvinyloxazolidones and poiyvinylimidazoles
or
mixtures thereof.
Addition of such polymers also enhances the pferformance of the enzymes
according the invention.
a) Polyamine N-oxide polymers
The polyamine N-oxide polymers suitable for use contain units having the
following structure formula
P
(I) Ax
I
R
wherein P is a polymerisable unit, whereto the R-N-O group can be attached
to or wherein the R-N-O group forms part of the polymerisable unit or
a combination of both.
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WO 99/57259 PCT/IJS99/09409
53
0 0 0
II II II
A is NC, CO, C, -o-,-s-, -N- ; x is o or 1;
R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or
alicyclic groups or any combination thereof whereto the nitrogen of
the N-O group can be attached or whE~rein the nitrogen of the N-O
group is part of these groups.
The N-O group can be represented by the following general structures
O O
I I
(R1)x -N- (R2)y =N- (R1)x
I
(R3)z
wherein R1, R2, and R3 are aliphatic groups, aromatic, heterocyclic or
alicyclic
groups or combinations thereof, x or/and y orland z is 0 or 1 and
wherein the nitrogen of the N-O group cain be attached or wherein the
nitrogen of the N-O group forms part of these groups.
The N-O group can be part of the polymerisable unit (P) or can be attached to
the polymeric backbone or a combination of both.
Suitable poiyamine N-oxides wherein the N-O group forms part of the
polymerisable unit comprise polyamine N-oxides wherein R is selected from
aliphatic, aromatic, alicyclic or heterocyclic groups.
One class of said polyamine N-oxides comprises the group of polyamine N-
oxides wherein the nitrogen of the N-O group forms part of the R-group.
Preferred polyamine N-oxides are those wherein R is a heterocyclic group such
as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, puinoline, acridine
and
derivatives thereof.
Another class of said polyamine N-oxides comprises the group of polyamine N-
oxides wherein the nitrogen of the N-O group is attached to the R-group.
Other suitable polyamine N-oxides are the polyamiine oxides whereto the N-O
group is attached to the polymerisable unit.
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Preferred class of these polyamine N-oxides are the polyamine N-oxides having
the general formula (I) wherein R is an aromatic, h~eterocyclic or alicyclic
groups
wherein the nitrogen of the N-0 functional group is part of said R group.
Examples of these classes are polyamine oxides wherein R is a heterocyclic
compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
Another preferred class of polyamine N-oxides are the polyamine oxides having
the general formula (I) wherein R are aromatic, hcsterocyclic or alicyciic
groups
wherein the nitrogen of the N-0 functional group is attached to said R groups.
Examples of these classes are polyamine oxidea wherein R groups can be
aromatic such as phenyl.
Any polymer backbone can be used as long as the amine oxide polymer formed
is water-soluble and has dye transfer inhibiting properties. Examples of
suitable
polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers,
polyamide, polyimides, polyacrylates and mixtures thereof.
The amine N-oxide polymers of the present invention typically have a ratio of
amine to the amine N-oxide of 10:1 to 1:1000000. I-lowever the amount of amine
oxide groups present in the polyamine oxide polymer can be varied by
appropriate copolymerization or by appropriate degree of N-oxidation.
Preferably, the ratio of amine to amine N-oxide is firom 2:3 to 1:1000000.
More
preferably from 1:4 to 1:1000000, most preferably from 1:7 to 1:1000000. The
polymers of the present invention actually encompass random or block
copolymers where one monomer type is an amine N-oxide and the other
monomer type is either an amine N-oxide or not. The amine oxide unit of the
polyamine N-oxides has a PKa < 10, preferably PKa < 7, more preferred PKa <
6.
The polyamine oxides can be obtained in almost ainy degree of polymerisation.
The degree of polymerisation is not critical provided the material has the
desired
water-solubility and dye-suspending power.
Typically, the average molecular weight is within the range of 500 to
1000,000;
preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000, most
preferably from 3,000 to 20,000.
b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole
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The N-vinylimidazole N-vinylpyrrolidone polymers used in the present invention
have an average molecular weight range from 5,000-1,000,000, preferably from
5,000-200,000.
Highly preferred polymers for use in detergent compositions according to the
present invention comprise a polymer selected from N-vinylimidazole N-
vinylpyrrolidone copolymers wherein said polymer has an average molecular
weight range from 5,000 to 50,000 more preferably from 8,000 to 30,000, most
preferably from 10,000 to 20,000.
The average molecular weight range was determined by light scattering as
described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113;"Modern
Methods of Polymer Characterization".
Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an
average molecular weight range from 5,000 to 5C?,000; more preferably from
8,000 to 30,000; most preferably from 10,000 to 20,000.
The N-viny(imidazole N-vinylpyrrolidone copolymers characterized by having
said average molecular weight range provide excellent dye transfer inhibiting
properties while not adversely affecting the cleaning performance of detergent
compositions formulated therewith.
The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has
a molar ratio of N-viny(imidazole to N-vinylpyrrolidone from 1 to 0.2, more
preferably from 0.8 to 0.3, most preferably from 0.6 t~o 0.4 .
c) Polyvinylpyrrolidone
The detergent compositions of the present invention may also utilize
polyvinylpyrrolidone ("PVP") having an average molecular weight of from about
2,500 to about 400,000, preferably from about 5,000 to about 200,000, more
preferably from about 5,000 to about 50,000, and most preferably from about
5,000 to about 15,000. Suitable polyvinylpyrrolidone~s are commercially
vailable
from ISP Corporation, New York, NY and Montreal, Canada under the product
names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average
molecular weight of 40,000), PVP K-60 (average molecular weight of 160,000),
and PVP K-90 (average molecular weight of 360,000). Other suitable
polyvinylpyrrolidones which are commercially available from BASF Cooperation
include Sokalan HP 165 and Soka(an HP 12; polyvinylpyrrolidones known to
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56
persons skilled in the detergent held {see for example EP A-262,897 and EP A-
256,696).
d) Polyvinyloxazolidone
The detergent compositions of the present invention may also utilize
polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said
polyvinyloxazolidones have an average molecular weight of from about 2,500 to
about 400,000, preferably from about 5,000 to about 200,000, more preferably
from about 5,000 to about 50,000, and most preferably from about 5,000 to
about 15,000.
e) Polyvinylimidazole
The detergent compositions of the present iinvention may also utilize
polyvinylimidazole as polymeric dye transfer inhibiting agent. Said
polyvinylimidazoles have an average of about 2,500 to about 400,000,
preferably from about 5,000 to about 200,000, mores preferably from about
5,000
to about 50,000, and most preferably from about 5,000 to about 15,000.
f) Cross-linked polymers
Cross-linked polymers are polymers whose backbone are interconnected to a
certain degree; these links can be of chemical or physical nature, possibly
with
active groups n the backbone or on branches; cross-linked polymers have been
described in the Journal of Polymer Science, volume 22, pages 1035-1039.
In one embodiment, the cross-linked polymers are rr~ade in such a way that
they
form a three-dimensional rigid structure, which can entrap dyes in the pores
formed by the three-dimensional structure. In another embodiment, the cross-
tinked polymers entrap the dyes by swelling.
Such cross-linked polymers are described in the co-pending patent application
94870213.9
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Method of washing
The compositions of the invention may be used in essentially any washing,
cleaning andlor fabric care methods, including soaking methods, pre-treatment
methods, methods with rinsing steps for which a sE:parate rinse aid
composition
may be added and post-treatment methods.
The process described herein comprises contacting fabrics with a laundering
solution in the usual manner and exemplified hereunder. A conventional laundry
method comprises treating soiled fabric with an aqueous liquid having
dissolved
or dispensed therein an effective amount of the laundry detergent andlor
fabric
care composition. The process of the invention is conveniently carried out in
the
course of the cleaning process. The method of cleaning is preferably carried
out
at 5°C to 95°C, especially between 10°C and 6Ci°C.
The pH of the treatment
solution is preferably from 7 to 12.
The following examples are meant to exemplify compositions of the present
invention, but are not necessarily meant to limit or otherwise define the
scope of
the invention.
In the detergent compositions, the enzymes levels are expressed by pure
enzyme by weight of the total composition and unless otherwise specified, the
detergent ingredients are expressed by weight of the total compositions. The
abbreviated component identifications therein have the following meanings:
Sodium linear 011_13 alkyl benzene sulphonate.
TAS : Sodium tallow alkyl sulphaite.
CxyAS ; Sodium C1x - C1y alkyl sullfate.
CxySAS ; Sodium C1x - C1y secondary (2,3) alkyl sulfate.
CxyEz : C1x - C1y predominantly linear primary alcohol
condensed with an average of z moles of ethylene
oxide.
CxyEzS : C1x - C1y sodium alkyl sulfate condensed with
an
average of z moles of ethyf~ene oxide.
QAS : R2.N+(CH3)2(C2H4~H) with R2 = C12-C14~
QAS 1 : R2~N+(CH3)2(C2H4~H) wilth R2 = Cg-011.
APA ~ Cg_1 p amido propyl dimethyl amine.
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Soap : Sodium linear alkyl carbo~;ylate derived from
a 80/20
mixture of tallow and coconut fatty acids.
STS : Sodium toluene sulphonat:e.
CFAA : C12-C14 alkyl N-methyl glucamide.
TFAA ; C1 g-C' g alkyl N-methyl glucamide.
TPKFA : C12-C14 topped whole cut fatty acids.
DEQA : Di-(tallow-oxy-ethyl) dimetlhyl ammonium chloride.
DEQA (2) : Di-(soft-tallowyloxyethyl) hydroxyethyl methyl
ammonium
methylsulfate.
DTDMAMS : Ditalllow dimethyl ammonin.~m methylsulfate.
SDASA : 1:2 ratio of stearyldimethyl amineariple-pressed
stearic
acid.
Silicate ; Amorphous Sodium Silicate (Si~2:Na20 ratio
= 1.6-3.2).
Zeolite A : Hydrated Sodium Aluminosilicate of formula
Nal2(A102Si02)12. 27H2;0 having a primary particle
size in the range from 0.1 to 10 micrometers
(Weight
expressed on an anhydrous basis).
Na-SKS-6 ; Crystalline layered silicate of formula 8-Na2Si205.
Citrate : Tri-sodium citrate dihydratE~ of activity 86.4%
with a
particle size distribution between 425 and 850
micrometres.
Citric : Anhydrous citric acid.
Borate : Sodium borate
Carbonate : Anhydrous sodium carbonate with a particle
size
between 200 and 900 micrometres.
Bicarbonate : Anhydrous sodium hydrogen carbonate with a
particle
size distribution between 400 and 1200 micrometres.
Sulphate : Anhydrous sodium sulphate:.
Mg Sulphate : Anhydrous magnesium sulfate.
STPP : Sodium tripolyphosphate.
TSPP : Tetrasodium pyrophosphate.
M~AA : Random copolymer of 4:1 acrylatelmaleate, average
molecular weight about 70,1700-80,000.
MAIAA 1 : Random copolymer of 6:4 a~crylatelmaleate,
average
molecular weight about 10,t)00.
I,
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AA : Sodium poiyacrylate polymer of average malecular
weight 4,500:
PB1 : Anhydrous sodium perborate monohydrate of nominal
formula NaB02.H202.
PB4 : Sodium perborate tetrahy~drate of nominal formula
NaB02.3H20. H202.
Percarbonate : Anhydrous sodium percarbonate of nominal formula
2Na2C03.3H202 .
TAED : Tetraacetylethylenediamine.
NOBS : Nonanoyloxybenzene sulfonate in the form of the sodium
salt.
NACA-OBS : {6-nonamidocaproyl) oxybenzene sulfonate.
DTPA : Diethylene triamine penta;acetic acid.
HEDP : 1,1-hydroxyethane diphosphonic acid.
DETPMP : Diethyltriamine penta (me~thylene) phosphonate,
marketed by Monsanto under the Trade name bequest
2060.
EDDS : Ethylenediamine-N,N'-disuccinic acid, (S,S)
isomer in the
form of its sodium salt
Photoaetivated : Sulfonated zinc phtalocyanine encapsulated
in dextrin
Bleach soluble polymer.
Photoactivated : Sulfonated alumino phtalocyanine encapsulated
in
Bleach 1 dextrin soluble polymer.
Protease : Proteolytic enzyme sold under the tradename
Savinase,
Alcalase, Durazym by Novo Nordisk AIS, Maxacal,
Maxapem sold by Gist-Brocades and proteases
described in patents W091/06637 andlor W095110591
andlor EP 251 446.
Amylase : Amylolytic enzyme sold under the tradename
Purafact
Ox AmR described in WO 94/18314, W096105295
sold
by Genencor; Termamyl~,. Fungamyl~ and Duramyl~,
all available from Novo Nordisk A!S and those
described
in WO95126397.
Lipase : Lipolytic enzyme sold undE~r the tradename
Lipolase,
Lipolase Ultra by Novo Nordisk AlS and Lipomax
by
Gist-Brocades.
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CBD-Cellulase : Cellulytic enzyme core derived tram the enzyme sold
under the tradename CarE:zyme by Novo Nordisk AlS
linked to the CBD of the CenC cellulase of Cellulomonas
frmi, either the tandem CBDN1 N2 or the single CBDN1
or CBDN2 and/or linked to the CBD from the cellulase .
E3 of Thermomonospora ~Fusca; and/or
Cellulytic enzyme core derived from the enzyme sold
under the tradename Care:zyme by Novo Nordisk A/S
linked by the f-lumicola lns;olens family 45 cellulase linker
to the CBD of the CenC cE;llulase of Cellulomonas firm,
either the tandem CBDN11V2 or the single CBDN1 or
CBDN2; and/or
Cellulytic enzyme core derived from the enzyme sold
under the tradename Carezyme by Novo Nordisk AlS
linked by the E3 cellulase Thermomonospora fusca
linker to the CBD from the cellulase E3 of
Thermomonospora fusca.
Cellulase : Celluiytic enzyme sold undier the tradename Carezyme,
Endolase by Novo Nordisk A/S; and/or Clazinase,
Puradex HAI, EGIII cellula:;e from Trichoderma reseei by
Genencor.
CMC : Sodium carboxymethyl cellfulose.
PVP : Polyvinyl polymer, with an average molecular weight of
60, 000.
PVNO : Polyvinylpyridine-N-Oxide, with an average molecular
weight of 50,000.
PVPVI : Copolymer of vinylimidazole and vinylpyrrolidone, with an
average molecular weight of 20,000.
Brightener 1 : Disodium 4,4'-bis(2-sulphoatyryl)biphenyl.
Brightener 2 : Disodium 4,4'-bis(4-anilino-~6-morpholino-1.3.5-triazin-2-
yl) stilbene-2:2'-disulfonate.
Silicone antifoam : Polydimethylsiloxane foam controller with siloxane-
oxyalkylene copolymer as dispersing agent with a ratio of
said foam controller to said dispersing agent of 10:1 to
100:1.
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Suds Suppressor : 12% Silicone/silica, 18% stearyl alcoho1,70% starch in
granular form.
Opacifer : Water based monostyren~e latex mixture, sold by BASF
Aktiengesellschaft under ilhe tradename Lytron 621.
SRP 1 : Anionically end capped poly esters.
SRP 2 : niethoxylated poly (1,2 propylene terephtalate) short
block polymer. .~
QEA : bis((C2H50)(C2H40)n)(C~H3) -N+-C6H12-N~'-(CH3)
bis((C2H50)-(C2H40))n, 'wherein n = from 20 to 30.
PEI : Polyethyleneimine with an average molecular weight of
1800 and an average ethoxylation degree of 7
ethyleneoxy residues per nitrogen.
SCS : Sodium cumene sulphona;te.
HMWPEO : High molecular weight polyethylene oxide.
PEGx : Polyethylene glycol, of a nnoiecular weight of x .
PEO : Polyethylene oxide, with an average molecular weight of
5,000.
TEPAE : TetreaethylenepentaaminE: ethoxylate.
Example 1
The following high density laundry detergent compositions were prepared
according to the present invention
I II III IV V VI
1-AS 8.0 8.0 8.0 2.0 6.0 6.0
TAS - 0.5 - 0.5 1.0 0.1
C46(S)AS 2.0 2.5 - - - _
C25AS - - - 7.0 4.5 5.5
C68AS 2.0 5.0 7.0 - -
C25E5 - - 3.4 10.0 4.6 4.6
C25E7 3.4 3.4 1.0 - - -
C25E3S - - - 2.0 5.0 4.5
QAS - 0.8 - .- _ _
QAS 1 - - - 0.8 0.5 1.0
Zeolite A 18.1 18.0 14.1 18.1 20.0 18.1
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62
r a ur rv v yr
Citric - - - 2.5 - 2.5
Carbonate 13.0 13.0 27.0 10.0 10.0 13.0
Na-SKS-6 - - - 10.0 - 10.0
Silicate 1.4 1.4 3.0 0.3 0.5 0.3
Citrate - 1.0 - 3.0 _ _
Sulfate 26.1 26.1 26.1 6.0 - -
Mg sulfate 0.3 _ - 0.2 - 0.2
M~~ 0.3 0.3 0.3 4.0 1.0 1.0
CMC 0.2 0.2 0.2 0.2 0.4 0.4
PB4 9.0 9.0 5.0 - - -
Percarbonate - - - - 18.0 18.0
TAED 1.5 0.4 1.5 - 3.9 4.2
NACA-OBS - 2.0 1.0 - - _
DETPMP 0.25 0.25 0.25 0.25 - -
SRP 1 - - - 0.2 - 0.2
EDDS - 0.25 0.4 - 0.5 0.5
CFAA - 1.0 - 2.0 - _
HEDP 0.3 0.3 0.3 0.3 0.4 0.4
QEA - - - 0.2 - 0.5
Protease 0.009 0.009 0.01 0.04 0.05 0.03
Amylase 0.002 0.002 0.002 0.006 0.008 0.008
CBD-cellulase 0.0007 0.01 0.0007 0.008 0.0008 0.001
Cellulase - - 0.0007 - 0.0007 0.0001
Lipase 0.006 - - 0.01 0.01 0.01
Photoactivated 15 15 15 - 20 20
bleach (ppm)
PVNO/PVPVI - - - 0.1 - -
Brightener 1 0.09 0.09 0.09 - 0.09 0.09
Perfume 0.3 0.3 0.3 0.4 0.4 0.4
Silicone antifoam0.5 0.5 0.5 - 0.3 0..3
Density in g/litre850 850 850 850 850 850
Miscellaneous Up to 100%
and minors
Example 2
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The following granular laundry detergent compositions of particular utility
under
European machine wash conditions were prepared according to the present
invention
I II III IV V Vt
LAS 5.5 7.5 5.0 5.0 6.0 7.0
TAS 1.25 1.9 - 0.8 0.4 0.3
C24AS/C25AS - 2.2 5.0 5.0 5.0 2.2
C25E3S - 0.8 1.0 1.5 3.0 1.0
C45E7 3.25 = - - - 3.0
TFAA _ _ 2.0 - - _
C25E5 - 5.5 - - - _
QAS 0.8 - - - .. _
QAS 1 - 0.7 1.0 0.5 1.0 0.7
STPP 19.7 - - - - -
Zeolite A - 19.5 25.0 19.5 20.0 17.0
NaSKS-6/citric ~- 10.6 - 10.6 - -
acid
(79:21 )
Na-SKS-6 - - 9.0 - 10.0 10.0
Carbonate 6.1 21.4 9.0 10.0 10.0 18.0
Bicarbonate - 2.0 7.0 5.0 - 2.0
Silicate 6.8 - - 0.3 0.5 -
Citrate - - 4.0 4.0 -
Sulfate 39.8 - - 5.0 ~ - 12.0
Mg sulfate - - 0.1 0.2 0.2
MAIAA 0.5 1.6 3.0 4.0 1.0 1.0
CMC 0.2 0.4 1.0 1.0 0.4 0.4
PB4 5.0 12.7 - _ _ _
Percarbonate - - - - 18.0 15.0
TAED 0.5 3.1 - - 5.0 -
NACA-OBS 1.0 3.5 - - - 2.5
DETPMP 0.25 0.2 0.3 0.4 - 0.2
HEDP - 0.3 - 0.3 0.3 0.3
QEA - - 1.0 'I.0 1.0 -
Protease 0.009 0.03 0.03 0.05 0.05 0.02
Lipase 0.003 0.003 0.006 0.006 0.006 0.004
CBD-cellulase 0.01 0.005 0.005 0.005 0.01 0.008
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I I1 III IV V VI
Cellulase 0.0006 - 0.0005 - - 0.0007
Amylase 0.002 0.002 0.006 0.006 0.01 0.003
PVNOIPVPVI - - 0.2 0.2 - -
PVP 0.9 1.3 - _ - 0.9
SRP 1 - - 0.2 0.2 0.2 -
Photoactivated 15 27 - - 20 20
bleach (ppm)
Photoactivated 15 -: - - -
bleach 1 (ppm)
Brightener 1 0.08 0.2 - - 0:09 0.15
Brightener 2 - 0.04 - - _ _
Perfume 0.3 0:5 0.4 0.3 0.4 0.3
Silicone antifoam 0.5 2.4 0.3 0.5 0.3 2.0
Density in gllitre 750 750 750 750 750 750
Miscellaneous and minors Up i :o 100%
Example 3
The following detergent formulations ility European
of particular ut under machine
wash conditions were prepared ntion
according to the present inve
I II III IV
Blown Powder
LAS 6.0 5.0 11.0 6.0
TAS 2.0 - - 2.0
Zeoiite A 24.0 - - 20.0
STPP - 27.0 24.0 -
Sulfate 4.0 6.0 13.0 -
MAJAA 1.0 4.0 6.0 2.0
Silicate 1.0 7.0 3.0 3.0
CMC 1.0 1.0 ~ 0.5 0.6
Brightener 1 0.2 0.2 0.2 0.2
Silicone antifoam 1.0 1.0 1.0 0:3
DETPMP 0.4 0.4 0.2 0.4
Spray On
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WO 99/5759 PCT/iJS99/09409
I II III IV
Brightener 0.02 - - 0.02
C45E7 - - - 5,0
C45E2 2.5 2.5 2.0
C45E3 2.6 2.5 2.0 -
Perfume 0.5 0.3 0.5 0.2
Silicone antifoam 0.3 0.3 0.3 -
Dry additives
QEA - _ - 1.0
EDDS 0.3 - -
Sulfate 2.0 3.0 5.0 10.0
Carbonate 6.0 13.0 15.0 14.0
Citric 2.5 - - 2,0
QAS 1 0.5 - - 0.5
Na-SKS-6 '! 0.0 - - -
Percarbonate 18.5 - -
PB4 - 18.0 10.0 21.5
TAED 2.0 2.0 - 2.D
NACA-OBS 3.0 2.0 4.0 -
CBD-cellulase 0.0005 0.01 0.005 0.01
Cellulase 0.0004 - - 0.0008
Protease 0.03 0.03 0.03 0.03
Lipase 0.008 0.008 0.008 0.004
Amylase 0.003 0.003 0.003 0.006
Brightener 1 0.05 - - 0.05
Miscellaneous and Up to
minors 100%
Example 4
The following granular preparedaccording
detergent formulations to the
were
present invention
I 11 Ill IV V VI
Blown Powder
LAS 23.0 8.0 7.0 9.0 7.0 7.0
TAS - - - - 1.0 -
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66
I II Ill IV V VI
c45AS s.o s.o 5.o s.o - _
C45AES - 1.0 1.0 1.0 - -
C45E35 - - - - 2.0 4.0
Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0
MA/AA - 0.5 - - - 2.0
MA/AA 1 7.0 - _ _ _ -
AA - 3.0 3.0 2.0 3.0 3.0
Sulfate 5.0 5.3 14.3 11.0 15.0 19.3
Silicate 10.0 1.0 1.0 1.0 1.0 1.0
Carbonate 15.0 20.0 10.0 20.7 8.0 6.0
PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0
DTPA - 0.9 0.5 - - 0,
5
Brightener 2 0.3 0.2 0.3 - 0.1 0.3
Spray On
C45E7 - 2.0 - - 2.0 2.0
C25E9 3.0 - - - _ _
C23E9 - - 1.5 2.0 - 2.0
Perfume 0.3 0.3 0.3 2.0 0.3 0.3
Agglomerates
C45AS ~- 5.0 5.0 2.0 - 5_0
LAS - 2.0 2.0 - - 2.0
Zeolite A - 7.5 7.5 8.0 - 7.5
Carbonate - 4.0 4.0 5.0 - 4.0
PEG 4000 - 0.5 0.5 - - 0.5
Misc (Water etc.) - 2.0 2.0 2:0 - 2.0
Dry additives
QAS - - _ - 1.0 -
Citric - - - _ 2.0 -
PB4 - - - - 12.0 1.0
PB1 4.0 1.0 3.0 2.0 - _
Percarbonate - - - - 2.0 10.0
Carbonate - 5.3 1.8 - 4.0 4.0
NOBS 4.0 - 6.0 - - 0.6
Methyl cellulose 0.2 - - _ _ -
Na-SKS-6 8.0 - - _ _ _
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I II III IV V VI
sTS - - 2. a - 1.0 -
Culmene sulfonic - 1.0 - - - 2.0
acid
Protease 0.02 0.02 0.02 0.01 0.02 0.02
Lipase 0.004 - 0.004 - 0.004 0.008
Amylase 0.003 - 0.002 - 0.003 -
CB~-cellulase 0.0005 0.01 0.0005 0.01 0.01 0.0005
Celiulase - - a.o005 0.0007 - 0.0008
PVPVI - - - - 0.5 0.1
PVP - - _ - 0.5 -
PVNO - - 0.5 0.3 - -
QEA - - - - 1.0 -
SRP 1 0.2 0.5 0.3 - 0.2 -
Silicone antifoam0.2 0.4 0.2 0.4 0.1 -
Mg sulfate - - 0.2 - 0.2 -
Miscellaneous Up ~to 100%
and minors
Example 5
The following nil bleach-containing detergentformulations of particular
use in the
washing of coloured clothingre prepared
we according
to the
present
invention
I II III
Blown Powder
Zeolite A 15.0 15.0 -
Sulfate - ;5.0 -
LAS 3.0 :3.0 -
DETPMP 0.4 17.5 -
CIVIC 0.4 t).4 -
MA/AA 4.0 4.0 -
Agglomerates
C45AS - - 11.0
LAS 6.0 fi.0 -
TAS 3.0 2.0 -
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I ll Ill
Silicate 4.0 ~4.0 -
Zeolite A 10.0 15.0 13.0
CMC - - 0.5
MA/AA - - 2.0
Carbonate 9.0 7.0 7.0
Spray-on
Perfume 0.3 0.3 0.5
C45E7 4:0 ~L0 4.0
C25E3 2.0 2.0 2.0
Dry additives
MA/AA - - 3.0
Na-SKS-6 - - 12.0
Citrate 10.0 - 8,p
Bicarbonate 7.0 3.0 5.0
Carbonate 8.0 5.0 7.0
PVPVUPVNO 0.5 (1i.5 0.5
Protease 0.03 0.02 0.05
Lipase 0.008 0.t708 0.008
Amylase 0.01 0.01 '0.01
CBD-cellulase 0.0005 0.01 0.005
Ceiluiase 0.0008 O.t)01 -
Silicone antifoam 5.0 5.0 5.0
Sulfate - 9.0 -
Density (gllitre) 700 7n0 700
Miscellaneous and minors Up tc> 100%
Exam~ole fi
The following detergent prepared .according
formulations were to the present
invention
I II III IV
Base granule
Zeolite A 30.0 22.0 24.0 10.0
Sulfate 10.0 5.0 10.0 7.0
MA/AA 3.0 - - -
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I II III IV
AA - 1.6 2.0 -
MA/AA 1 - 12.0 - 6.0
LAS 14.0 10.0 9.0 20.0
C45AS 8.0 7.0 9.0 7.0
C45AES - 1.0 1.0
Silicate - 1.0 0.5 10.0
Soap - 2.0 -
Brightener 1 0.2 0.2 0.2 0.2
Carbonate 6.0 9.0 10.0 1 ~.0
PEG 4000 - 1.0 1.5 -
DTPA - 0.4 -
Spray On
C25E9 - - - 5.0
C45E7 1.0 1.0 - _
C23E9 - 1.0 2.5
Perfume 0.2 0.3 0.3
Dry additives
Carbonate 5.0 10.0 18.0 8.0
PVPVI/PVNO 0.5 - 0.3 -
Protease 0.03 0.03 0.03 0.02
Lipase 0.008 - - 0.008
Amylase 0.002 - - 0.002
CBD-cellulase 0.01 0.0005 0.01 0.0005
Cellulase 0.0002 0.0005 - _
NOBS - 4.0 - 4.5
PB 1 1.0 5.0 1.5 6.0
Sulfate 4.0 5.0 - 5.0
SRP 1 - 0.4 - _
Suds suppresser - 0.5 0.5
Miscellaneous and minors Up to 100%
Example 7
The following granular detergent formulations werE; prepared according to the
present invention
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I II lil
Blown Powder
Zeolite A 20.0 - 15.0
STPP - 20.0 -
Sodium sulfate - - 5.0
Carbonate - - 5.0
TAS - - 1.0
LAS 6.0 6.0 6.0
C68AS 2.0 2.0 -
Silicate 3.0 8.0
MA/AA 4.0 2.0 2.0
CMC 0.6 0.6 0.2
Brightener 1 0.2 0.2 0.1
DETPMP 0.4 0.4 0.1
STS - - 1.0
Spray On
c45E7 5.0 5.0 4.a
Silicone antifoam0.3 0.3 0.1
Perfume 0.2 0.2 0.3
Dry additives
QEA - - 1.0
Carbonate 14.0 9.0 10.0
PB1 1.5 2.0 -
PB4 18.5 13.0 13.0
TAED 2.0 2.0 2.0
QAS - - 1.0
Photoactivated 15 ppm 15 ppm 15 ppm
bleach
Na-SKS-6 - - 3.0
Protease 0.03 0.03 0.007
Lipase 0.004 0.004 0.004
Amylase 0.006 0.006 0.003
CBD-cellulase 0.0005 0.01 0.005
Cellulase 0.0002 - -
Sulfate 10.0 20.0 5.0
Density (g/litre) 700 700 700
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Miscellaneous and minors Up to 100%
Exami~le 8
The following detergent formulations were prepared according to the present
invention
Blown Powder
Zeolite A 15.0 15.0 15.0
Sulfate - 5.0
LAS 3.0 3.0 3.0
QAS - 1.5 1.5
DETPMP 0.4 0.2 0.4
EDDS - 0.4 0.2
CMC 0.4 0.4 0.4
MAIAA 4.0 2.0 2.0
Agglomerate
LAS 5.0 5.0 5.0
TAS 2.0 2.0 1.0
Silicate 3.0 3.0 4.0
Zeolite A 8.0 8.0 8.0
Carbonate 8.0 8.0 4.0
Spray 4n
Perfume 0.3 0.3 0.3
C45E7 2.0 2.0 2.0
C25E3 2.0 - -
~ry Additives
Citrate 5.0 - 2.0
Bicarbonate - 3.0 -
Carbonate 8.0 15.0 10.0
TAED 6.0 2.0 5.0
PB1 14.0 7.0 10.0
PEO - - 0_2
Bentonite clay- - 10.0
Protease 0.03 0.03 0.03
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I II III
Lipase 0.008 0.008 0.008
CBD-cellulase 0.005 0.01 0.0005
Cellulase - 0.0007 0.001
Amylase 0.01 0.01 0.01
Silicone antifoam 5.0 5.0 5.0
Sulfate - 3.0 -
Density (gllitre) 850 850 850
Miscellaneous and minors Up to 100%
Example 9
The following detergent formulations were prepared according to the present
invention
I II III IV'
LAS 18.0 14.0 24.0 20.0
QAS 0.7 1.0 - 0.7
TFAA - 1, 0 _
C23E56.5 - - 1.0 -
C45E7 - 1.0 _ _
C45E3S 1.0 2.5 1.0 -
STPP 32.0 18.0 30.0 22.0
Silicate ~ 9.0 5.0 9.0 8.0
Carbonate 11.0 7.5 10.0 5.0
Bicarbonate - 7,5 _ _
PB1 3.0 1.0 - -
PB4 - 1.0 -
NOBS 2.0 1.0 - -
DETPMP - 1.0 - -
DTPA 0.5 - 0.2 0.3
SRP 1 0.3 0.2 - 0,1
M~~ 1.0 1.5 2.0 0.5
CMC 0.8 0.4 0.4 0.2
PEI - - 0.4 -
Sulfate 20.0 10.0 20.0 30.0
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I II III IV
Mg sulfate 0.2 - 0.4 0.9
Protease 0.03 0.03 0.02 0.02
Amylase 0.00$ 0.007 - 0.004
Lipase 0.004 - 0.002 -
CBD-cellulase 0.0005 0.01 0.0005 0.005
Cellulase - - 0.003 0.001
Photoactivated bleach 30 ppm 20 ppm - 10
ppm
Perfume 0.3 0.3 0.1 0.2
Brightener 1/2 0.05 0.02 0.08 0.1
Miscellaneous and Minors up to 100%
Example 10
The following liquid detergent formulations were prepared according to the
present invention (Levels are given in parts per weiight)
I II III IV V
LAS 11.5 8.8 - 3.9 -
C25E2.5S - 3.0 18.0 - 16.0
C45E2.25S 11.5 3.0 - 15.7 -
C23E9 - 2.7 1.8 2.0 1.0
C23E7 3.2 - - - -
CFAA - - 5.2 - 3.1
TPKFA 1.6 - 2.0 0.5 2.0
Citric (50%) 6.5 1.2 2.5 4.4 2.5
Ca formate 0.1 0.06 0.1 - -
Na formate 0.5 0.06 0.1 0.05 0.05
SCS 4.0 1.0 3.0 1.2 -
Borate 0.6 - 3.0 2.0 2.9
Na hydroxide 5.8 2.0 3.5 3.7 2.7
Ethanol 1.75 1.0 3.6 4.2 2.9
1,2 Propanediol 3.3 2.0 8.0 7.9 5.3
Monoethanolamine 3.0 1.5 1.3 2.5 0.8
TE PAE 1.6 - 1.3 1.2 1:2
Protease 0.03 0.01 0.03 0.02 0.02
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II III IV V
Lipase - - 0.002 - -
Amylase - - - 0.002 -
CBD-cellulase 0.0005 0.01 0.005 0.01 0.005
Cellulase 0.001 - - 0.0005 -
SRP 1 0.2 - 0.1 -
DTPA _ _ 0.3 _
PVNO - - 0.3 - 0.2
Brightener 1 0.2 0.07 0.1 - _
Silicone antifoam 0.04 0.02 0.1 0.1 0.1
Miscellaneous and Up to 100%
water
Example 11
The following liquid detergent formulations werE: prepared according to the
present invention (Levels are given in parts per weiight)
I II III IV
~S 10.0 '13.0 9.0 -
C25AS 4.0 1.0 2.0 '10.0
C25E3S 1.0 _ _ 3.0
C25E7 6.0 8.0 13.0 2.5
TFAA - - - 4.5
APA - 1.4 - _
TPKFA 2.0 - 13.0 7.0
Citric 2.0 3.0 1.0 1.5
Dodecenyl ! tetradecenyl 12.0 10.0 - -
succinic
acid
Rapeseed fatty acid 4.0 2.0 1.0
Ethanol
4.0 ~4.0 7.0 2.0
1,2 Propanediol 4.0 4.0 2.0 ~,0
Monoethanolamine - _ _ 5.0
Triethanolamine _ _ g.~
TEPAE 0.5 - 0.5 0.2
DETPMP 1.0 'I.0 0.5 1.p
Protease 0.02 0.02 0.01 0.008
Lipase - 0.002 - 0.002
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Amylase 0.004 0.004 0.01 0.008
CBD-cellulase 0.0005 i).0008 0.003 0.002
Cellulase - 0.0007 0.0007 -
SRP 2 0.3 - 0.3 0.1
Boric acid 0.1 0.2 1.0 2.0
Ca chloride - 0.02 - 0.01
Brightener 1 - 0.4 - _
Suds suppressor ~ 0.1 0.3 - 0.1
Opacifier 0.5 0.4 - 0.3
NaOH up to pH 8.0 8.0 7.6 7.7
Miscellaneous and water Up to 100%
Example 12
The following liquid detergent formulations werE: prepared according to the
present invention (Levels are given in parts per weight)
I II III iV
~S 25.0 - _ _
C25AS - 13.0 18.0 15.0
C25E3S - s>_.0 2.0 4.0
C25E7 - - 4.0 4.0
TFAA - Ei.O 8.0 8.0
APA 3.0 1.0 2.0 -
TPKFA - 1.5.0 11.0 11.0
Citric 1.0 1.0 1.0 1.0
Dodeceny! J tetradecenyi 15.0 - - ,_
succinic
acid
Rapeseed fatty acid 1.0 _ 3.5
Ethanol 7.0 2.0 3.0 2.0
1,2 Propanediol 6.0 8.0 10.0 13.0
Monoethanalamine _ _ 9.0 9.0
TEPAE - ~- 0.4 0.3
DETPMP 2.0 1..2 1.0
Protease 0.08 0.02 0.01 0.02
Lipase - -~ 0.003 0.003
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I II III IV
Amylase 0.004 0.01 0.01 0.01
CBD-cellulase 0.0003 0.0006 0.004 0.003
Cellulase 0.0003 - _ _
SRP 2 - - 0.2 0.1
Boric acid 1.0 1.5 2.5 2.5
Bentonite clay 4.0 4.0 - _
Brightener 1 0.1 0.2 0.3
Suds suppressor 0.4 - _ _
Opacifier 0,8 0.7 - -
NaOH up to pH 8.0 7.5 8.0 g,2
Miscellaneous and wafer Up to 100%
Example 13
The following liquid detergent compositions were prepared according to the
present invention {Levels are given in parts by weic,~ht)
I It
~S 27.6 18.9
C45AS 13.8 5.9
C13E8 3.0 3.1
Oleic acid 3.4 2.5
Citric 5.4 5.4
Na hydroxide 0.4 3.6
Ca Formate 0.2 0.1
Na Formate _ 0.5
Ethanol 7.0 -
Monoethanolamine 16.5 g_0
1,2 propanediol 5.9 5.5
Xylene sulfonic acid - 2.4
TEPAE 1.5 0.8
Protease 0.05 0.02
CBD-cellulase 0.0003 0.0006
Cellulase - 0.0002
PEG _ 0.7
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I II
Brightener 2 0.4 0.1
Perfume 0.5 0.3
Miscellaneous and water Up to 100%
Example 14
The following granular fabric detergent compositions which provide
'°softening
through the wash" capability were prepared according to the present invention
t II
C45AS - 10.0
~S 7.fi
C6$AS 1.3 -
C45E7 4.0
C25E3 - 5.0
Coco-alkyl-dimethyl hydroxy-1.4 ~ 1.0
ethyl ammonium chloride
Citrate 5.0 3.0
Na-SKS-6 - 11.0
Zeolite A 15.0 15.0
M~~ 4.0 4.0
DETPMP 0.4 0.4
PB1 15.0 -
Percarbonate - 15.0
TAED 5.0 5.0
Smectite clay 10.0 10.0
HMWPEO - 0.1
Protease 0.02 0.01
Lipase 0.02 0.01
Amylase 0.03 0.005
CBD-celluiase 0.01 0.0009
Cellulase 0.005 0.001
Silicate 3.0 5,0
Carbonate 10.0 10.0
Suds suppressor
1.0 4,0
i
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I II
CMC
0.:?
0.1
WateNminors Up to 1100%
Example 15
The following rinse added fabric softener compositions were prepared according
to the present invention
I II
DEQA (2) 20.0 20.0
CBD-celluiase 0.001 0.001
Cellulase _ 0.0005
HCL 0.03 0.03
Antifoam agent 0.01 0.01
Blue dye 25ppm 25ppm
CaCl2
0.20
0.20
Pertume 0.90 0.90
Miscellaneous and water Up to 1 Ci0%
Exam~te 10
The following fabric softener and fabric
dryer added conditioner
compositions
were prepared according to the present
invention
I II lil IV V
DEQA 2.6 19.0 - _ _
DEQA(2) _
_
- - 51.8
DTMAMS - - - 26.0 -
SDASA - - 70.0 42.0 40.2
Stearic acid of IV=0 0.3 - _ _
Neodol45-13 _ _ 13.0 - _
Hydrochloride acid 0.02 0.02 - _
Ethanol _ _ 1.0 - -
CBD-celluiase 0.0001 0.001 0.0005 0.005 0.0003
Celiulase 0.001 - 0.0007 - 0.0003
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I II III IV V
Perfume 1.0 1.0 0.75 1.0 1.5
Glycoperse S-20 - - - - 15.4
Glycerol monostearate- - - 26.0 -
Digeranyl Succinate - - 0.38 - _
Silicone antifoam 0.01 0.01 - _ _
Electrolyte - 0.1 _ _ _
Clay - - - 3.0 -
Dye 10ppm 25ppm 0.01 - -
Water and minors 100% 100% - - _
Example 17
The following laundry bar detergent compositions were prepared according to
the present invention
I 11 III VI V Ill VI V
~S - - 19.0 15.0 :? 6.75 8. -
1.0 8
C28AS 30.0 13.5 - - - 15.75 11.2 22.5
Na Laurate 2.5 9.0 - - - _ _ _
Zeolite A 2.0 1.25 - - - 1.25 1.25 1.25
Carbonate 20.0 3.0 13.0 8.0 'I0.0 15.0 15.0 10.0
Ca Carbonate27.5 39.0 35.0 - - 40.0 - 40.0
Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0
TSPP 5.0 - _ _ - 5.0 2.5 -
STPP 5.0 15.0 10.0 - - 7.0 8.0 10.0
Bentonite - 10.0 - - :5.0 - - -
clay
DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7
CMC - 1.0 1.0 1.0 1.0 - - 1.0
Talc - - 10.0 15.0 10.0 - - -
Silicate - - 4.0 5.0 3.0 - - -
PVN4 0.02 0.03 - 0.01 - 0.02 - _
MA/AA 0.4 1.0 - - t).2 0.4 0.5 0.4
SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3
Amylase - - 0.01 - _ - 0.002 -
Protease - 0.004 - 0.003 0.003 - - 0.003
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I II III Vl V III VI V
Lipase - 0.002 - 0.002 - - _ _
CBD-cellulase.0008 .0003 .0002 .0003 .0003 .0002 .0005 .0005
Cellulase - - - .0005 - .0002 .0004 -
PEO - 0.2 - 0.2 0.3 - - 0.3
Perfume 1.0 0.5 0.3 0.2 0.4 - - 0.4
Mg sulfate - - 3.0 3.0 3.0 - - -
Brightener 0.15 0.1 0.15 - - - - 0.1
Photoactivated- 15.0 15:0 15.0 '15.0 - - 15.0
bleach (ppm)
Example 18
The following pre- or post treatment compositions were prepared in accord with
the present invention
I Il III ~IV
DEQA (2) - - 20.0 20.0
CBD-cellulase 0.0008 0.002 0.001 0.001
Cellufase 0.0005 - 0.0005 -
HCL - - 0.03 0.03
Antifoam agent - - 0.01 0.01
Biue dye 25ppm 25ppm 25ppm 25ppm
CaCl2 - - 0.20 0.20
Perfume 0.90 0.90 0.90 0.90
Water / minors Up to '! 00/~
